ID APT_ACISJ Reviewed; 184 AA. AC A1WDB0; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Ajs_4134; OS Acidovorax sp. (strain JS42). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=232721; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JS42; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., RA Richardson P.; RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000539; ABM44235.1; -; Genomic_DNA. DR RefSeq; WP_011807211.1; NC_008782.1. DR ProteinModelPortal; A1WDB0; -. DR STRING; 232721.Ajs_4134; -. DR EnsemblBacteria; ABM44235; ABM44235; Ajs_4134. DR KEGG; ajs:Ajs_4134; -. DR PATRIC; 20693727; VBIAciSp27161_4363. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; ASP232721:GHWE-4198-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000645; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 184 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321331. SQ SEQUENCE 184 AA; 20130 MW; A9F4D24953225B7B CRC64; MTALSVNDYL RQHIRTVPDW PAPGVQFRDI TPLLQNPKVF RVLIDAFVHR YMDRALRPDV VAGLDARGFI LGAVVAYELN VGFVPIRKKG KLPFTTVEET YELEYGSATV ELHADAVQPG DRVLLIDDLI ATGGTMMAGK KLLEKLGATV MEGAAIVDLP ELGGSERLRA SGLPLYTLVD FSGH // ID APT_ACAM1 Reviewed; 170 AA. AC B0CBF7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=AM1_2945; OS Acaryochloris marina (strain MBIC 11017). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Acaryochloris. OX NCBI_TaxID=329726; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBIC 11017; RX PubMed=18252824; DOI=10.1073/pnas.0709772105; RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., RA Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., RA Mimuro M., Blankenship R.E., Touchman J.W.; RT "Niche adaptation and genome expansion in the chlorophyll d-producing RT cyanobacterium Acaryochloris marina."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000828; ABW27942.1; -; Genomic_DNA. DR RefSeq; WP_012163376.1; NC_009925.1. DR ProteinModelPortal; B0CBF7; -. DR STRING; 329726.AM1_2945; -. DR EnsemblBacteria; ABW27942; ABW27942; AM1_2945. DR KEGG; amr:AM1_2945; -. DR PATRIC; 20620170; VBIAcaMar40141_2713. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; AMAR329726:GCZJ-2934-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000268; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000073786. SQ SEQUENCE 170 AA; 18590 MW; D79D2B202D6BABB9 CRC64; MDLKSLIRDI PDFPKPGILF RDITTLLQNP DGLRYVIDQF TEDYREQSID YVVGIESRGF IFGAPLAYQL GAGFVPVRKP GKLPAAIHAQ EYELEYGTDR LEIHQDACPA GSRVLVVDDL LATGGTAAAT AQLLAPLNCT LVGFGFIIEL TGLAGRQKLP DCHINALVEY // ID APT_ACIC5 Reviewed; 181 AA. AC C1F3T2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 11-NOV-2015, entry version 46. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=ACP_2871; OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670 / OS NBRC 15755 / NCIMB 13165 / 161). OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=240015; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51196 / DSM 11244 / JCM 7670 / NBRC 15755 / NCIMB 13165 / RC 161; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., RA Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., RA Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., RA Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C., RA Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., RA Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., RA Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., RA Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., RA Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001472; ACO32691.1; -; Genomic_DNA. DR RefSeq; WP_015897928.1; NC_012483.1. DR ProteinModelPortal; C1F3T2; -. DR STRING; 240015.ACP_2871; -. DR EnsemblBacteria; ACO32691; ACO32691; ACP_2871. DR KEGG; aca:ACP_2871; -. DR PATRIC; 20668985; VBIAciCap40988_2756. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; ACAP240015:GKF4-2817-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002207; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 181 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116225. SQ SEQUENCE 181 AA; 20138 MW; 4B12099CCD586216 CRC64; MQPTHSVNCE PLKSLVRTVP DFPKPGILFY DITTLLKDRQ GFAKLIDALA EHYIGKNIDL VLGIEARGFI FGPALAYRLN AGFVPVRKPR KLPARTVRVT YDLEYGSDTL EIHEDAIEPG QRIVLVDDLL ATGGTMEATV KLVRQLGGEI AGLAFAVELD FLKGRERFPD LDVFSLLHYS E // ID APT_ACICJ Reviewed; 171 AA. AC A5FVJ4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Acry_0401; OS Acidiphilium cryptum (strain JF-5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=349163; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JF-5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T., RA Richardson P.; RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000697; ABQ29626.1; -; Genomic_DNA. DR RefSeq; WP_011941503.1; NC_009484.1. DR ProteinModelPortal; A5FVJ4; -. DR STRING; 349163.Acry_0401; -. DR EnsemblBacteria; ABQ29626; ABQ29626; Acry_0401. DR KEGG; acr:Acry_0401; -. DR PATRIC; 20645764; VBIAciCry6074_0884. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; ACRY349163:GHET-408-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000245; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 171 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000251. SQ SEQUENCE 171 AA; 18572 MW; 0C069CB9F757A5EA CRC64; MNLKDHIRGI PDFPKPGILF YDISTLIRHA DAWQVAMGRL AKVVRAHHPD LLAGVESRGF ILAAPLALKL GCGFIMLRKR GKLPGATVGY DYDLEYGQDR IEIQADAVQP GQRVVVVDDL LATGGTMAAG IKLLRKVGAE VPAAAALIEL AFLKGRDRLD VPFEALVSYD Q // ID APT_ALKOO Reviewed; 172 AA. AC A8MGN2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 1. DT 11-NOV-2015, entry version 52. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Clos_1715; OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii OS (strain OhILAs)). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Alkaliphilus. OX NCBI_TaxID=350688; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OhILAs; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., RA Ranganathan M., Basu P., Richardson P.; RT "Complete genome of Alkaliphilus oremlandii OhILAs."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000853; ABW19255.1; -; Genomic_DNA. DR RefSeq; WP_012159567.1; NC_009922.1. DR ProteinModelPortal; A8MGN2; -. DR STRING; 350688.Clos_1715; -. DR EnsemblBacteria; ABW19255; ABW19255; Clos_1715. DR KEGG; aoe:Clos_1715; -. DR PATRIC; 20868678; VBIAlkOre124042_1795. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; AORE350688:GHBG-1745-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000269; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000057028. SQ SEQUENCE 172 AA; 18935 MW; A91BA7197F4F1F67 CRC64; MDLKSKIRQI EGFPKEGISF KDITTVLKEG EALQYVTDQL TEQLKDLNID IIVGPEARGF LVGTPVAYKL GVGFVPVRKP GKLPAETLTY EYELEYGTDS LQIHKDSIRP GQRVAIVDDL LATGGTVLAT AKMVEALGGQ VVSMNFLIEL TGLKGRDILK GYEIKSLVEY EF // ID APT_ASHGO Reviewed; 187 AA. AC Q756E2; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Adenine phosphoribosyltransferase; DE Short=APRT; DE EC=2.4.2.7; GN Name=APT1; OrderedLocusNames=AER325W; OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Eremothecium gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=284811; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient RT Saccharomyces cerevisiae genome."; RL Science 304:304-307(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=23749448; DOI=10.1534/g3.112.002881; RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.; RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type RT loci, numerous translocations, lack of transposons, and distinct gene RT duplications."; RL G3 (Bethesda) 3:1225-1239(2013). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016818; AAS53005.1; -; Genomic_DNA. DR RefSeq; NP_985181.1; NM_210535.1. DR ProteinModelPortal; Q756E2; -. DR SMR; Q756E2; 1-178. DR EnsemblFungi; AAS53005; AAS53005; AGOS_AER325W. DR GeneID; 4621394; -. DR KEGG; ago:AGOS_AER325W; -. DR HOGENOM; HOG000036776; -. DR InParanoid; Q756E2; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG7WT4CC; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000591; Chromosome V. DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006168; P:adenine salvage; IEA:InterPro. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Magnesium; KW Metal-binding; Nucleus; Purine salvage; Reference proteome; KW Transferase. FT CHAIN 1 187 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000227898. FT NP_BIND 133 137 AMP. {ECO:0000250}. SQ SEQUENCE 187 AA; 20434 MW; ECCB97F1DF3DE7F1 CRC64; MSINEYAKEL KAALAQYPNF PKEGVLFEDF LPIFRSPQLF QKLIDAFKMH LAEAFPETKI DYLVGLESRG FLFGPSLALA IGAGFVPVRK AGKLPGQVVK TTYVKEYEED VFEMQVDSIP VGATVVVVDD ILATGGSAGA AGDLIKQLGA TILEFIFVME LDFLKGREKL QAPVFTLLQG QEEALGN // ID APT_BACC0 Reviewed; 170 AA. AC B7JPZ4; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 11-NOV-2015, entry version 47. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BCAH820_4488; OS Bacillus cereus (strain AH820). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=405535; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH820; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus AH820."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001283; ACK91178.1; -; Genomic_DNA. DR RefSeq; WP_000346214.1; NC_011773.1. DR ProteinModelPortal; B7JPZ4; -. DR EnsemblBacteria; ACK91178; ACK91178; BCAH820_4488. DR KEGG; bcu:BCAH820_4488; -. DR PATRIC; 18845949; VBIBacCer122868_4481. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BCER405535:GHSL-4502-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001363; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116162. SQ SEQUENCE 170 AA; 18644 MW; 148BA98F47CF8FFC CRC64; MDFKQHIAIV PDYPKEGIVF KDITPLMNDG KAYKAATDAI VEYAKERDID LVVGPEARGF IIGCPVSYAL EVGFAPVRKL GKLPREVITV DYGKEYGKDV LTIHKDAIKP GQRVLITDDL LATGGTIEAT IKLVEELGGV VAGIAFLVEL TYLDGRKMLD GYDVLVLEKY // ID APT_ACTP2 Reviewed; 179 AA. AC A3MYY8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=APL_0266; OS Actinobacillus pleuropneumoniae serotype 5b (strain L20). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=416269; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L20; RX PubMed=18065534; DOI=10.1128/JB.01845-07; RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., RA Nash J.H.E.; RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20 RT (serotype 5b)."; RL J. Bacteriol. 190:1495-1496(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000569; ABN73374.1; -; Genomic_DNA. DR RefSeq; WP_005596155.1; NC_009053.1. DR ProteinModelPortal; A3MYY8; -. DR SMR; A3MYY8; 3-179. DR STRING; 416269.APL_0266; -. DR EnsemblBacteria; ABN73374; ABN73374; APL_0266. DR GeneID; 4850209; -. DR KEGG; apl:APL_0266; -. DR PATRIC; 20745336; VBIActPle94089_0272. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; APLE416269:GHV7-276-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001432; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 179 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000252. SQ SEQUENCE 179 AA; 19491 MW; 35ADB04389F50485 CRC64; MNQLDLIKSS IKSIPDYPKA GIIFRDITSL LEVPEAFKAT VDAIVAEFKD KGITKVVGTE SRGFIFGAPV ALALGVPFVL VRKPKKLPRA VISQSYALEY GEDTLEIHLD SVKENDNVLM VDDLLATGGT IDATAKLIRR LGGKVEHAAF VIWLPDLGGK ERLEKEGINS FTLVEFAGH // ID APT_BACCR Reviewed; 170 AA. AC Q817X3; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=BC_4402; OS Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / OS NCIMB 9373 / NRRL B-3711). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=226900; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL RC B-3711; RX PubMed=12721630; DOI=10.1038/nature01582; RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D., RA Overbeek R., Kyrpides N.C.; RT "Genome sequence of Bacillus cereus and comparative analysis with RT Bacillus anthracis."; RL Nature 423:87-91(2003). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016877; AAP11315.1; -; Genomic_DNA. DR RefSeq; NP_834114.1; NC_004722.1. DR RefSeq; WP_000346215.1; NC_004722.1. DR ProteinModelPortal; Q817X3; -. DR STRING; 226900.BC4402; -. DR PRIDE; Q817X3; -. DR EnsemblBacteria; AAP11315; AAP11315; BC_4402. DR GeneID; 1206747; -. DR KEGG; bce:BC4402; -. DR PATRIC; 32604903; VBIBacCer54481_4553. DR eggNOG; COG0503; LUCA. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BCER226900:GJEU-4398-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001417; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149347. SQ SEQUENCE 170 AA; 18630 MW; A491A98F47D58FF7 CRC64; MDFKQHIAIV PDYPKEGIVF KDITPLMNDG KAYKAATDAI VEYAKERDID VVVGPEARGF IIGCPVSYAL EVGFAPVRKL GKLPREVITV DYGKEYGKDV LTIHKDAIKP GQRVLITDDL LATGGTIEAT IKLVEELGGV VAGIAFLVEL TYLDGRKMLD GYDVLVLEKY // ID APT_ALISL Reviewed; 181 AA. AC B6EJ41; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 20-JAN-2016, entry version 48. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=VSAL_I1084; OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain OS LFI1238)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=316275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LFI1238; RX PubMed=19099551; DOI=10.1186/1471-2164-9-616; RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., RA Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., RA Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.; RT "The genome sequence of the fish pathogen Aliivibrio salmonicida RT strain LFI1238 shows extensive evidence of gene decay."; RL BMC Genomics 9:616-616(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FM178379; CAQ78769.1; -; Genomic_DNA. DR RefSeq; WP_012549839.1; NC_011312.1. DR ProteinModelPortal; B6EJ41; -. DR STRING; 316275.VSAL_I1084; -. DR EnsemblBacteria; CAQ78769; CAQ78769; VSAL_I1084. DR KEGG; vsa:VSAL_I1084; -. DR PATRIC; 20852382; VBIAliSal95923_1215. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001730; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 181 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088951. SQ SEQUENCE 181 AA; 19604 MW; 46DD00B29553054D CRC64; MSTETLELIK NSIKSVPDYP KAGIMFRDVT SLMEDPKAYQ ATIQLLVEKY KQGGFTKIVG TEARGFLFGA PLALELGVGF VPVRKPGKLP RPTIAQTYDL EYGTDTLEIH TDAIVEGDKV LVVDDLLATG GTIEATVKLI RQLGGDVQHA AFVINLPEIG GETRLEGLGL NVYSICEFPG H // ID APT_BACCQ Reviewed; 170 AA. AC B9IYY2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 11-NOV-2015, entry version 47. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BCQ_4194; OS Bacillus cereus (strain Q1). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=361100; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Q1; RX PubMed=19060151; DOI=10.1128/JB.01629-08; RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., RA Xu X., Xue Y., Zhu Y., Jin Q.; RT "Complete genome sequence of the extremophilic Bacillus cereus strain RT Q1 with industrial applications."; RL J. Bacteriol. 191:1120-1121(2009). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000227; ACM14621.1; -; Genomic_DNA. DR RefSeq; WP_000346214.1; NC_011969.1. DR ProteinModelPortal; B9IYY2; -. DR EnsemblBacteria; ACM14621; ACM14621; BCQ_4194. DR KEGG; bcq:BCQ_4194; -. DR PATRIC; 18916145; VBIBacCer120424_4239. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BCER361100:GJ7M-4182-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000441; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116230. SQ SEQUENCE 170 AA; 18644 MW; 148BA98F47CF8FFC CRC64; MDFKQHIAIV PDYPKEGIVF KDITPLMNDG KAYKAATDAI VEYAKERDID LVVGPEARGF IIGCPVSYAL EVGFAPVRKL GKLPREVITV DYGKEYGKDV LTIHKDAIKP GQRVLITDDL LATGGTIEAT IKLVEELGGV VAGIAFLVEL TYLDGRKMLD GYDVLVLEKY // ID APT_BACSK Reviewed; 171 AA. AC Q5WHQ1; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 20-JAN-2016, entry version 73. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=ABC1569; OS Bacillus clausii (strain KSM-K16). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=66692; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16; RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii RT KSM-K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006627; BAD64104.1; -; Genomic_DNA. DR RefSeq; WP_011246413.1; NC_006582.1. DR ProteinModelPortal; Q5WHQ1; -. DR STRING; 66692.ABC1569; -. DR EnsemblBacteria; BAD64104; BAD64104; ABC1569. DR KEGG; bcl:ABC1569; -. DR PATRIC; 18922596; VBIBacCla58185_1666. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BCLA66692:GHMP-1632-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001168; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 171 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149353. SQ SEQUENCE 171 AA; 19023 MW; 4754535E09C8255D CRC64; MDYKQYITIV EDWPQEGIRF KDITTLMQNG TAYKRAVEEL AVYAKEKQAD VIVGPEARGF VVGCPIATEL EIGFVPVRKK GKLPREVIEA NYGLEYGKDC LTIHKDSIQP GQRVVITDDL LATGGTIEAT AKMVEQLGGK VVGIAFLIEL AYIGGRDKLK QYDLFSLMSY E // ID APT_ACIAC Reviewed; 184 AA. AC A1TWI0; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Aave_4787; OS Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. OS citrulli). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=397945; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AAC00-1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., RA Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., RA Richardson P.; RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000512; ABM35318.1; -; Genomic_DNA. DR RefSeq; WP_011797784.1; NC_008752.1. DR ProteinModelPortal; A1TWI0; -. DR STRING; 397945.Aave_4787; -. DR EnsemblBacteria; ABM35318; ABM35318; Aave_4787. DR KEGG; aav:Aave_4787; -. DR PATRIC; 20684859; VBIAciCit38535_4879. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; ACIT397945:GI5W-4849-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002596; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 184 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321330. SQ SEQUENCE 184 AA; 20270 MW; B76B0E6EDACF09C8 CRC64; MQDLSVNEYL RQYIRTVPDW PAAGVQFRDI TPLLQDPKVF RVLIDAFVHR YMDRALRPDV VAGLDARGFI LGAVVAYELN VGFVPIRKKG KLPFTTVEET YELEYGSATV ELHADAVKPG DRVLLIDDLI ATGGTMMAGR RLLERLGATV TEGAAIVDLP ELGGSSRLRE SGLPLYTLVD FAGH // ID APT_BACAA Reviewed; 170 AA. AC C3P995; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 11-NOV-2015, entry version 45. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BAA_4655; OS Bacillus anthracis (strain A0248). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=592021; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A0248; RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., RA Sims D., Brettin T.; RT "Genome sequence of Bacillus anthracis A0248."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001598; ACQ48197.1; -; Genomic_DNA. DR RefSeq; WP_000346214.1; NC_012659.1. DR ProteinModelPortal; C3P995; -. DR EnsemblBacteria; ACQ48197; ACQ48197; BAA_4655. DR KEGG; bai:BAA_4655; -. DR PATRIC; 18775203; VBIBacAnt132916_4914. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BANT592021:GJAQ-4604-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116228. SQ SEQUENCE 170 AA; 18644 MW; 148BA98F47CF8FFC CRC64; MDFKQHIAIV PDYPKEGIVF KDITPLMNDG KAYKAATDAI VEYAKERDID LVVGPEARGF IIGCPVSYAL EVGFAPVRKL GKLPREVITV DYGKEYGKDV LTIHKDAIKP GQRVLITDDL LATGGTIEAT IKLVEELGGV VAGIAFLVEL TYLDGRKMLD GYDVLVLEKY // ID APT_BIFLD Reviewed; 193 AA. AC B3DRY2; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 11-NOV-2015, entry version 51. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BLD_0455; OS Bifidobacterium longum (strain DJO10A). OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=205913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJO10A; RX PubMed=18505588; DOI=10.1186/1471-2164-9-247; RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., RA Slesarev A.I., Weimer B., O'Sullivan D.J.; RT "Comparative genomic analysis of the gut bacterium Bifidobacterium RT longum reveals loci susceptible to deletion during pure culture RT growth."; RL BMC Genomics 9:247-247(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000605; ACD97901.1; -; Genomic_DNA. DR RefSeq; WP_007052860.1; NC_010816.1. DR ProteinModelPortal; B3DRY2; -. DR EnsemblBacteria; ACD97901; ACD97901; BLD_0455. DR KEGG; blj:BLD_0455; -. DR PATRIC; 21113844; VBIBifLon134794_0471. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; VHALCAF; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BLON205913:GJB4-473-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002419; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 193 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088954. SQ SEQUENCE 193 AA; 20223 MW; 78D4F35FE3D04872 CRC64; MAQSDITIDA LSKVGQQDAE YLVSLVRSVP GFPKEGIIFR DFMPVLADPK GLKILLKALE EALPVSPSEF DSIAGLESRG FLFGPAMAAH LGKGFIAVRK AGKLPPETIG ESYDLEYGTA SVEIETDAVQ AGKRVLIVDD LIATGGTAKA ATDLIEKAGG TVVGFSFVMR LDGLDGLDKL DGKPSSSLIA MPA // ID APT_BACWK Reviewed; 170 AA. AC A9VIN4; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BcerKBAB4_4255; OS Bacillus weihenstephanensis (strain KBAB4). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KBAB4; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., RA Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000903; ABY45414.1; -; Genomic_DNA. DR RefSeq; WP_002015305.1; NC_010184.1. DR ProteinModelPortal; A9VIN4; -. DR STRING; 315730.BcerKBAB4_4255; -. DR EnsemblBacteria; ABY45414; ABY45414; BcerKBAB4_4255. DR GeneID; 22938581; -. DR KEGG; bwe:BcerKBAB4_4255; -. DR PATRIC; 19013176; VBIBacWei55973_4903. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BWEI315730:GHRU-4371-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002154; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088953. SQ SEQUENCE 170 AA; 18588 MW; BC2A02B08A54F1F2 CRC64; MDFKQHIAIV PDYPKEGIVF KDITPLMNDG KAYKAATDAI VEYANKRDID VVVGPEARGF IIGCPVSYAL EVGFAPVRKL GKLPREVITV DYGKEYGTDV LTIHKDAIKP GQRVLITDDL LATGGTIEAT IKLVEELGGV VAGIAFLVEL TYLDGRKMLD GYDVLVLEKY // ID APT_BORBZ Reviewed; 176 AA. AC B7J0M3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 17-FEB-2016, entry version 44. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BbuZS7_0806; OS Borrelia burgdorferi (strain ZS7). OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella. OX NCBI_TaxID=445985; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZS7; RX PubMed=20935092; DOI=10.1128/JB.01158-10; RA Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J., RA Mongodin E.F., Luft B.J.; RT "Whole-genome sequences of thirteen isolates of Borrelia RT burgdorferi."; RL J. Bacteriol. 193:1018-1020(2011). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001205; ACK74678.1; -; Genomic_DNA. DR RefSeq; WP_012597342.1; NC_011728.1. DR ProteinModelPortal; B7J0M3; -. DR EnsemblBacteria; ACK74678; ACK74678; BbuZS7_0806. DR KEGG; bbz:BbuZS7_0806; -. DR PATRIC; 20561041; VBIBorBur54821_0911. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; VHALCAF; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BBUR445985:GKEU-802-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000006901; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 176 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116167. SQ SEQUENCE 176 AA; 20204 MW; 0E653342DD969F1D CRC64; MKNKTEYYDQ FISKIPNFPK KGVLFYDITS VLLKPEVYSS LINEVYSFYN FKKIDCIAVV ESRGYLIGAP LSLKMQLPLV LIRKEGKLPR EVFSEEYELE YGFGRIEVHK DDVRMYSNIL LIDDILATGG TLKSSAILLE RAGGKVKDIF CFIELCAING RQSLESYEVN SLVRYN // ID APT_BORBP Reviewed; 176 AA. AC Q65ZZ7; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 17-FEB-2016, entry version 72. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=BG0801; OS Borreliella bavariensis (strain ATCC BAA-2496 / DSM 23469 / PBi) OS (Borrelia bavariensis). OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella. OX NCBI_TaxID=290434; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-2496 / DSM 23469 / PBi; RX PubMed=15547252; DOI=10.1093/nar/gkh953; RA Gloeckner G., Lehmann R., Romualdi A., Pradella S., RA Schulte-Spechtel U., Schilhabel M., Wilske B., Suehnel J., Platzer M.; RT "Comparative analysis of the Borrelia garinii genome."; RL Nucleic Acids Res. 32:6038-6046(2004). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000013; AAU07624.1; -; Genomic_DNA. DR RefSeq; WP_011194071.1; NC_006156.1. DR ProteinModelPortal; Q65ZZ7; -. DR STRING; 290434.BG0801; -. DR EnsemblBacteria; AAU07624; AAU07624; BG0801. DR KEGG; bga:BG0801; -. DR PATRIC; 20567177; VBIBorGar102262_0886. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BGAR290434:BG0801-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002276; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 176 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149360. SQ SEQUENCE 176 AA; 20150 MW; 2DCB9DC5F1023DA2 CRC64; MKNKTEYYDQ FIAKVPDFPK KGVLFYDITS VLLKPEVYTS LINEAYSFYN LKKIDCIAVV ESRGYLIGAP LSLKMQLPLV LIRKEGKLPR EVFGEEYELE YGFGKIEVHK DDVRMYSNIL LIDDILATGG TLKSSAILLE RAGGRVKDIF CFIELCGING RRILEDYDVN SLVRYN // ID APT_BACTN Reviewed; 176 AA. AC Q8A2N8; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=BT_3267; OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC OS 10582 / E50 / VPI-5482). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=226186; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482; RX PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., RA Chiang H.C., Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015928; AAO78373.1; -; Genomic_DNA. DR RefSeq; NP_812179.1; NC_004663.1. DR RefSeq; WP_008762874.1; NC_004663.1. DR ProteinModelPortal; Q8A2N8; -. DR STRING; 226186.BT_3267; -. DR PaxDb; Q8A2N8; -. DR EnsemblBacteria; AAO78373; AAO78373; BT_3267. DR GeneID; 1075872; -. DR KEGG; bth:BT_3267; -. DR PATRIC; 21061541; VBIBacThe70966_3332. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR InParanoid; Q8A2N8; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BTHE226186:GJXV-3332-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001414; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 176 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149355. SQ SEQUENCE 176 AA; 19781 MW; 948DA2AF96700127 CRC64; MIMSKETLIK SIREIPDFPI PGILFYDVTT LFKDPWCLQE LSNIMFEMYK DKGITKVVGI ESRGFIMGPI LATRLNAGFI PIRKPGKLPA EVIEESYDKE YGTDTVQIHK DALDENDVVL LHDDLLATGG TMKAACELVK KLKPKKVYVN FIIELKDLNG KSVFGDDVEV ESVLTL // ID APT_BORBU Reviewed; 176 AA. AC O51718; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=BB_0777; OS Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM OS 4680). OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella. OX NCBI_TaxID=224326; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680; RX PubMed=9403685; DOI=10.1038/37551; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., RA Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., RA Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., RA Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., RA Roberts K.M., Hatch B., Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia RT burgdorferi."; RL Nature 390:580-586(1997). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000783; AAC67130.1; -; Genomic_DNA. DR PIR; H70196; H70196. DR RefSeq; NP_212911.1; NC_001318.1. DR RefSeq; WP_002656149.1; NC_001318.1. DR ProteinModelPortal; O51718; -. DR STRING; 224326.BB_0777; -. DR EnsemblBacteria; AAC67130; AAC67130; BB_0777. DR GeneID; 1195634; -. DR KEGG; bbu:BB_0777; -. DR PATRIC; 20558217; VBIBorBur75917_1169. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR KO; K00759; -. DR OMA; VHALCAF; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BBUR224326:G9SO-787-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 176 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149359. SQ SEQUENCE 176 AA; 20173 MW; 19420342DD8F861D CRC64; MKNKTEYYDQ FISKIPNFPK KGVLFYDITS VLLKPEVYSS LINEVYSFYN FKKIDCIAVV ESRGYLIGAP LSLKMQLPLV LIRKEGKLPR EVFSEEYELE YGFGRIEVHK DDVRTYSNIL LIDDILATGG TLKSSAILLE RAGGKVKDIF CFIELCAING RQSLESYEVN SLVRYN // ID APT_BURCC Reviewed; 188 AA. AC B1JYN1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Bcenmc03_2795; OS Burkholderia cenocepacia (strain MC0-3). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=406425; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC0-3; RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0- RT 3."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000958; ACA91954.1; -; Genomic_DNA. DR RefSeq; WP_012329235.1; NC_010508.1. DR ProteinModelPortal; B1JYN1; -. DR EnsemblBacteria; ACA91954; ACA91954; Bcenmc03_2795. DR KEGG; bcm:Bcenmc03_2795; -. DR PATRIC; 19092836; VBIBurCen61509_2900. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BCEN406425:GHD9-2868-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002169; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 188 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088957. SQ SEQUENCE 188 AA; 20401 MW; B3A60E9F50E7F485 CRC64; MPHSSPGAPL DPVAFIHSQI RTVPDWPQPG VQFRDITTLL QSPKALRILV DLFVERYVDA KLDYVAGLDA RGFIIAPIVA YELSVGFVPI RKVGKLPYKT RSESYDLEYG SATVEIHEDA CKPGDRVIIM DDLIATGGTM MAGRNLLQRL GAEVVEGAAI IDLPDLGGST LLRNAGLPVY TVTEFAGH // ID APT_AGARV Reviewed; 174 AA. AC C4ZF43; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 17-FEB-2016, entry version 45. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=EUBREC_2433; OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC OS 5835 / VPI 0990) (Eubacterium rectale). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Agathobacter. OX NCBI_TaxID=515619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / VPI 0990; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001107; ACR76164.1; -; Genomic_DNA. DR RefSeq; WP_012743258.1; NC_012781.1. DR ProteinModelPortal; C4ZF43; -. DR EnsemblBacteria; ACR76164; ACR76164; EUBREC_2433. DR KEGG; ere:EUBREC_2433; -. DR PATRIC; 21872949; VBIEubRec107985_2114. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; EREC515619:GHMX-2422-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001477; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 174 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000201663. SQ SEQUENCE 174 AA; 19078 MW; D9A32F762112C24C CRC64; MKTVKDYIRT IPDFPEKGIM FRDVTSVIQD ADGLKLAIDE MIKRLDGLDF DVIAGAESRG FVFGMPIAYA LHKPFVMVRK AGKLPCETVS KTYDLEYGTA TIEMHKDSVK PGQKVVLVDD LIATGGTMQA AAELVEELGG EVVKMLFLIE LAGLNGRKLL SKYDVDAVVS YDGK // ID APT_BRASB Reviewed; 179 AA. AC A5EE90; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BBta_2310; OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=288000; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BTAi1 / ATCC BAA-1182; RX PubMed=17540897; DOI=10.1126/science.1139548; RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C., RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., RA Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., RA Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P., RA Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A., RA Medigue C., Sadowsky M.; RT "Legumes symbioses: absence of nod genes in photosynthetic RT bradyrhizobia."; RL Science 316:1307-1312(2007). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000494; ABQ34484.1; -; Genomic_DNA. DR RefSeq; WP_012042512.1; NC_009485.1. DR ProteinModelPortal; A5EE90; -. DR STRING; 288000.BBta_2310; -. DR EnsemblBacteria; ABQ34484; ABQ34484; BBta_2310. DR KEGG; bbt:BBta_2310; -. DR PATRIC; 21205495; VBIBraSp29847_2432. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BSP288000:GJBR-2210-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000246; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 179 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000261. SQ SEQUENCE 179 AA; 19225 MW; 7A8DD3785074E7B0 CRC64; MTFDLDIKNT VRTIPDYPKP GILFRDITTL LADARAFRRA VDELVHPWAG SKIDKVAGIE ARGFILGGAV AHQLSAGFVP IRKKGKLPHK TVSMSYALEY GTDEMEMHVD AVQPGERVIL VDDLIATGGT AEGAVKLLRQ IGATVVAACF IIDLPDLGGA AKLRALDVPV RALIAFEGH // ID APT_BRUA2 Reviewed; 181 AA. AC Q2YM57; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 11-NOV-2015, entry version 69. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BAB1_1556; OS Brucella abortus (strain 2308). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC -!- SEQUENCE CAUTION: CC Sequence=CAJ11512.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM040264; CAJ11512.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_002964645.1; NZ_KN046823.1. DR ProteinModelPortal; Q2YM57; -. DR SMR; Q2YM57; 8-181. DR PRIDE; Q2YM57; -. DR EnsemblBacteria; CAJ11512; CAJ11512; BAB1_1556. DR GeneID; 3788616; -. DR KEGG; bmf:BAB1_1556; -. DR PATRIC; 17846105; VBIBruMel86222_1614. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BABO359391:GKDV-1589-MONOMER; -. DR BioCyc; BMEL359391:GJOQ-1589-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002719; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 181 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321341. SQ SEQUENCE 181 AA; 19614 MW; 128ABF9D88C2A953 CRC64; MESGFKVTLK DAIRTIPDYP KPGVQFRDVT TLMGNAQAFR RAVDELVYPY AGNRIDKVAG IEARGFILGG AIAHQLSAGF VPIRKKGKLP RDTVRIAYSL EYGVDEMEMH RDAIEKGERV VLVDDLIATG GTAEAAAKLL LQMGAEIVAA CFIIDLPDLG GRKKLEALGL PVRTLVAFEG D // ID APT_BURP6 Reviewed; 187 AA. AC A3N5L9; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 11-NOV-2015, entry version 59. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BURPS668_0588; OS Burkholderia pseudomallei (strain 668). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320373; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=668; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC -!- SEQUENCE CAUTION: CC Sequence=ABN84827.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000570; ABN84827.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; A3N5L9; -. DR EnsemblBacteria; ABN84827; ABN84827; BURPS668_0588. DR KEGG; bpd:BURPS668_0588; -. DR PATRIC; 19247169; VBIBurPse82117_0559. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BPSE320373:GJ9C-587-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002153; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 187 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321348. SQ SEQUENCE 187 AA; 20266 MW; B4EEFCD2BBB344D1 CRC64; MMSTSDAPLD PVEFIHSRIR TVPDWPQPGV MFRDITPLLQ SAKALRVLVD LFVERYVDAN LDYIAGLDAR GFIIAPIVAY ELSVGFVPIR KVGKLPYATQ RESYALEYGT ATVEIHEDAC KPGDRVVIVD DLIATGGTMM AGKNLLERLG AVVVEGAAIV DLPDLGGSAL LREAGLPLYT VTEFPGH // ID APT_BREBN Reviewed; 170 AA. AC C0ZAP9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 20-JAN-2016, entry version 48. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BBR47_18810; OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599). OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=358681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=47 / JCM 6285 / NBRC 100599; RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W., RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S., RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., RA Yoshikawa H., Udaka S., Tanikawa S., Fujita N.; RT "Brevibacillus brevis strain 47, complete genome."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008955; BAH42858.1; -; Genomic_DNA. DR RefSeq; WP_012685596.1; NC_012491.1. DR ProteinModelPortal; C0ZAP9; -. DR STRING; 358681.BBR47_18810; -. DR EnsemblBacteria; BAH42858; BAH42858; BBR47_18810. DR KEGG; bbe:BBR47_18810; -. DR PATRIC; 21234074; VBIBreBre96763_1871. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BBRE358681:GHYS-1994-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001877; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116234. SQ SEQUENCE 170 AA; 18501 MW; 9E433FFD1765D848 CRC64; MDFKQYIRVI PDFPQPGIRF KDITTLLKDG PAYKAAIQDL AVFAREVQAD VIAGPEARGF VVGAPLSYEM GIGFVPIRKS GKLPYESIKA NYDLEYGKDA LAVHVDAIQP GQRVLIADDL LATGGTIETT INLIEQLGGK VVGAAFFIEL SYLDGRSKIG EIPIKSLVQY // ID APT_CAEEL Reviewed; 185 AA. AC P91455; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 16-MAR-2016, entry version 92. DE RecName: Full=Adenine phosphoribosyltransferase; DE Short=APRT; DE EC=2.4.2.7; GN ORFNames=T19B4.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Bristol N2; RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., RA Thierry-Mieg Y., Thierry-Mieg D., Thierry-Mieg J.; RT "The Caenorhabditis elegans transcriptome project, a complementary RT view of the genome."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FO080338; CCD62975.1; -; Genomic_DNA. DR EMBL; AF303266; AAG50224.1; -; mRNA. DR PIR; T25891; T25891. DR RefSeq; NP_491663.1; NM_059262.7. DR UniGene; Cel.35570; -. DR ProteinModelPortal; P91455; -. DR SMR; P91455; 17-171. DR STRING; 6239.T19B4.3.1; -. DR EPD; P91455; -. DR PaxDb; P91455; -. DR EnsemblMetazoa; T19B4.3; T19B4.3; WBGene00020557. DR GeneID; 172232; -. DR KEGG; cel:CELE_T19B4.3; -. DR UCSC; T19B4.3.1; c. elegans. DR CTD; 172232; -. DR WormBase; T19B4.3; CE13740; WBGene00020557; -. DR eggNOG; KOG1712; Eukaryota. DR eggNOG; COG0503; LUCA. DR GeneTree; ENSGT00390000017259; -. DR HOGENOM; HOG000036776; -. DR InParanoid; P91455; -. DR KO; K00759; -. DR OMA; VHALCAF; -. DR OrthoDB; EOG7FFMT9; -. DR PhylomeDB; P91455; -. DR Reactome; R-CEL-74217; Purine salvage. DR UniPathway; UPA00588; UER00646. DR NextBio; 874607; -. DR PRO; PR:P91455; -. DR Proteomes; UP000001940; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006168; P:adenine salvage; IEA:InterPro. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 185 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149511. SQ SEQUENCE 185 AA; 20210 MW; 91A984C4F770F268 CRC64; MTLPRFDQIR PKIEQHIREV KDFPKKGINF RDIMPLFTNP QLVNELCVVI ADHVRHTVGH VDSVAGLEAR GFLFGPQVAI QLGVPFVPIR KKGKLPGATI EASYVKEYGE DRVEIQEGAI KNGDIVFLID DLLATGGTLR AATDLVVKAG GKVGEAFVLI ELAPLNGRSK LPDVNLTTLI SYDSA // ID APT_BRUAB Reviewed; 181 AA. AC Q57BX7; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 11-NOV-2015, entry version 78. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BruAb1_1529; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., RA Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison RT to the highly similar genomes of Brucella melitensis and Brucella RT suis."; RL J. Bacteriol. 187:2715-2726(2005). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC -!- SEQUENCE CAUTION: CC Sequence=AAX74857.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017223; AAX74857.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_002964645.1; NC_006932.1. DR ProteinModelPortal; Q57BX7; -. DR SMR; Q57BX7; 8-181. DR PRIDE; Q57BX7; -. DR EnsemblBacteria; AAX74857; AAX74857; BruAb1_1529. DR GeneID; 3788616; -. DR KEGG; bmb:BruAb1_1529; -. DR PATRIC; 17824806; VBIBruAbo15061_1617. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BABO262698:GJC2-1560-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000540; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 181 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321340. SQ SEQUENCE 181 AA; 19614 MW; 128ABF9D88C2A953 CRC64; MESGFKVTLK DAIRTIPDYP KPGVQFRDVT TLMGNAQAFR RAVDELVYPY AGNRIDKVAG IEARGFILGG AIAHQLSAGF VPIRKKGKLP RDTVRIAYSL EYGVDEMEMH RDAIEKGERV VLVDDLIATG GTAEAAAKLL LQMGAEIVAA CFIIDLPDLG GRKKLEALGL PVRTLVAFEG D // ID APT_BRUSI Reviewed; 181 AA. AC B0CHX9; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 2. DT 11-NOV-2015, entry version 51. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BSUIS_A1599; OS Brucella suis (strain ATCC 23445 / NCTC 10510). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=470137; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23445 / NCTC 10510; RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., RA Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., RA Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., RA Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., RA Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., RA Munk C., Brettin T.S.; RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC -!- SEQUENCE CAUTION: CC Sequence=ABY38630.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000911; ABY38630.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_006071215.1; NC_010169.1. DR ProteinModelPortal; B0CHX9; -. DR SMR; B0CHX9; 8-181. DR EnsemblBacteria; ABY38630; ABY38630; BSUIS_A1599. DR KEGG; bmt:BSUIS_A1599; -. DR PATRIC; 17870784; VBIBruSui83806_3182. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BSUI470137:GJIC-1588-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000008545; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 181 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000329337. SQ SEQUENCE 181 AA; 19586 MW; F59CCEFA9EA5A94B CRC64; MESGFKVTLK DAIRTIPDYP KPGVQFRDVT TLMGNAQAFR RAVDELVYPY AGNRIDKVAG IEARGFILGG AIAHQLSAGF VPIRKKGKLP RDTARIAYSL EYGVDEMEMH RDAIEKGERV VLVDDLIATG GTAEAAAKLL LQMGAEIVAA CFIIDLPDLG GRKKLEALGL PVRTLVAFEG D // ID APT_BURM9 Reviewed; 206 AA. AC A2S6D4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BMA10229_A1521; OS Burkholderia mallei (strain NCTC 10229). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=412022; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10229; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000546; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; WP_004195202.1; NC_008836.1. DR ProteinModelPortal; A2S6D4; -. DR PATRIC; 19133998; VBIBurMal46188_3717. DR HOGENOM; HOG000036776; -. DR OMA; EDPRING; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BMAL412022:GJI8-1521-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002283; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 206 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321345. SQ SEQUENCE 206 AA; 22225 MW; 2C980CF31B1DE1A1 CRC64; MSSDRRTARD CSAVFFGEFH DVHVGRAARS RRVHSQPHPH GAGLAAARRD VSRHHAALQS AKALRVLVDL FVERYVDAKL DYIAGLDARG FIIAPIVAYE LSVGFVPIRK VGKLPYATQR ESYALEYGTA TVEIHEDACK PGDRVVIVDD LIATGGTMMA GKNLLERLGA VVVEGAAIVD LPDLGGSALL REAGLPLYTV TEFPGH // ID APT_BURPP Reviewed; 188 AA. AC B2SXI3; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 11-NOV-2015, entry version 49. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Bphyt_0603; OS Burkholderia phytofirmans (strain DSM 17436 / PsJN). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=398527; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17436 / PsJN; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Nowak J., Sessitsch A., Lazarovits G., Compant S., RA Barka E., Tiedje J.; RT "Complete sequence of chromosome 1 of Burkholderia phytofirmans RT PsJN."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001052; ACD15028.1; -; Genomic_DNA. DR RefSeq; WP_012431666.1; NC_010681.1. DR ProteinModelPortal; B2SXI3; -. DR STRING; 398527.Bphyt_0603; -. DR EnsemblBacteria; ACD15028; ACD15028; Bphyt_0603. DR KEGG; bpy:Bphyt_0603; -. DR PATRIC; 19211117; VBIBurPhy117947_4348. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BPHY398527:GJEX-606-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001739; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 188 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088960. SQ SEQUENCE 188 AA; 20431 MW; ECB97373E59CC8EF CRC64; MSNALASAPL DAADYIKSHI RTVPDWPQPG VQFRDITPLL QEPKSLRVLI DLFVQRYIDA KLDYIAGLDA RGFIIGPILA YELNLGFIPI RKAGKLPYKR VAQSYELEYG TATVEIHEDA CKPGDRIVII DDLIATGGTM MAGKILLERL GAVVVEGAAI IDLPELGGSK LLREGGLALY TVTGFDGH // ID APT_BURCA Reviewed; 188 AA. AC Q1BTI4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Bcen_2170; OS Burkholderia cenocepacia (strain AU 1054). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331271; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AU 1054; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., RA Konstantinidis K., Tiedje J.M., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia AU RT 1054."; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000378; ABF77071.1; -; Genomic_DNA. DR RefSeq; WP_011546233.1; NC_008060.1. DR ProteinModelPortal; Q1BTI4; -. DR SMR; Q1BTI4; 8-188. DR EnsemblBacteria; ABF77071; ABF77071; Bcen_2170. DR KEGG; bcn:Bcen_2170; -. DR PATRIC; 19048041; VBIBurCen11237_2264. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BCEN331271:GHKX-2216-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002400; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 188 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321342. SQ SEQUENCE 188 AA; 20421 MW; B3A613EB50E7F485 CRC64; MPHSSPGAPL DPVAFIHSQI RTVPDWPQPG VQFRDITTLL QSPKALRILV DLFVERYVDA KLDYVAGLDA RGFIIAPIVA YELSVGFVPI RKVGKLPYKT RSESYDLEYG SATVEIHEDA CKPGDRVIIM DDLIATGGTM MAGRNLLQRL GAEVVEGAAI IDLPDLGGST LLRNAGLTVY TVTEFSGH // ID APT_BURCH Reviewed; 188 AA. AC A0KAK7; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Bcen2424_2784; OS Burkholderia cenocepacia (strain HI2424). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=331272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI2424; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F., RA Konstantinidis K., Tiedje J.M., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia RT HI2424."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000458; ABK09534.1; -; Genomic_DNA. DR RefSeq; WP_011546233.1; NC_008542.1. DR ProteinModelPortal; A0KAK7; -. DR SMR; A0KAK7; 8-188. DR EnsemblBacteria; ABK09534; ABK09534; Bcen2424_2784. DR KEGG; bch:Bcen2424_2784; -. DR PATRIC; 19063019; VBIBurCen15205_2845. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BCEN331272:GHR7-2855-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase. FT CHAIN 1 188 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321343. SQ SEQUENCE 188 AA; 20421 MW; B3A613EB50E7F485 CRC64; MPHSSPGAPL DPVAFIHSQI RTVPDWPQPG VQFRDITTLL QSPKALRILV DLFVERYVDA KLDYVAGLDA RGFIIAPIVA YELSVGFVPI RKVGKLPYKT RSESYDLEYG SATVEIHEDA CKPGDRVIIM DDLIATGGTM MAGRNLLQRL GAEVVEGAAI IDLPDLGGST LLRNAGLTVY TVTEFSGH // ID APT_CAMFF Reviewed; 182 AA. AC A0RQ44; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CFF8240_1169; OS Campylobacter fetus subsp. fetus (strain 82-40). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=82-40; RA Fouts D.E., Nelson K.E.; RT "Sequence of Campylobacter fetus subsp. fetus 82-40."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000487; ABK82642.1; -; Genomic_DNA. DR RefSeq; WP_002849820.1; NC_008599.1. DR ProteinModelPortal; A0RQ44; -. DR EnsemblBacteria; ABK82642; ABK82642; CFF8240_1169. DR GeneID; 4539521; -. DR KEGG; cff:CFF8240_1169; -. DR PATRIC; 20036856; VBICamFet25865_1142. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CFET360106:GHTH-1167-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000760; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 182 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000268. SQ SEQUENCE 182 AA; 20317 MW; 79F0B011F54008EF CRC64; MKELSKFDKE YLLGTIRDIK NFPKPGIIFK DITTLLGNAK AFKFLLDHLE DRYKDENLDF IVGIESRGFI LGAALSARLN LGFVPVRKPN KLPYITISQK YSLEYGFDEV EMHIDAFDSI KNPKVLLVDD LIATGGTAKA SSQLLKKLGV NLVEACFLVD LVELGGSKEL KSECPVYSVL EV // ID APT_CHLAA Reviewed; 173 AA. AC A9WCV7; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Caur_0273; OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl). OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae; OC Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=324602; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl; RX PubMed=21714912; DOI=10.1186/1471-2164-12-334; RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.; RT "Complete genome sequence of the filamentous anoxygenic phototrophic RT bacterium Chloroflexus aurantiacus."; RL BMC Genomics 12:334-334(2011). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000909; ABY33526.1; -; Genomic_DNA. DR RefSeq; WP_012256182.1; NC_010175.1. DR RefSeq; YP_001633915.1; NC_010175.1. DR ProteinModelPortal; A9WCV7; -. DR STRING; 324602.Caur_0273; -. DR EnsemblBacteria; ABY33526; ABY33526; Caur_0273. DR GeneID; 5828030; -. DR KEGG; cau:Caur_0273; -. DR PATRIC; 21411058; VBIChlAur28763_0314. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR InParanoid; A9WCV7; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CAUR324602:GIXU-276-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002008; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 173 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000329338. SQ SEQUENCE 173 AA; 19242 MW; 18680CCD0004184A CRC64; MTRQDLASLI RNIPDFPIPG IQFKDITTLI GNGQAFSEVI DRLHERYQNQ QIDAVVGIES RGFIFSAPLA YRLGVGLVPI RKPGKLPAAT YQIEYQLEYG TNRLEIHRDA FQPGARVLVI DDLLATGGTI AAACDLIEMA GGQVAELAFV IELTFLNGRE RLRERPVFSL IQF // ID APT_BURXL Reviewed; 188 AA. AC Q145V4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Bxeno_A0347; ORFNames=Bxe_A4115; OS Burkholderia xenovorans (strain LB400). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=266265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LB400; RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., RA Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., RA Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M., RA Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., RA Tiedje J.M.; RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp RT genome shaped for versatility."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000270; ABE28885.1; -; Genomic_DNA. DR RefSeq; WP_011486714.1; NZ_CP008760.1. DR ProteinModelPortal; Q145V4; -. DR STRING; 266265.Bxe_A4115; -. DR EnsemblBacteria; ABE28885; ABE28885; Bxe_A4115. DR GeneID; 4005037; -. DR KEGG; bxb:DR64_1791; -. DR KEGG; bxe:Bxe_A4115; -. DR PATRIC; 19326053; VBIBurXen52548_0367. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BXEN266265:GJII-353-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001817; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 188 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321352. SQ SEQUENCE 188 AA; 20476 MW; BE68D2546FBE1ED2 CRC64; MSNALPSAPL DAADYIKSHI RTVPDWPEPG VQFRDITPLL QEPKSLRVLI DLFVQRYIDA KLDYIAGLDA RGFIIGPILA YELNLGFIPI RKAGKLPYNR LAQSYELEYG CATVEIHEDA CKPGDRVVII DDLIATGGTM MAGKILLERL GAVVVEGAAI IDLPELGGSK LLRDSGLALY TVTGFEGH // ID APT_CAMJE Reviewed; 182 AA. AC Q9PP06; Q0P9X2; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 20-JAN-2016, entry version 88. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=Cj0927; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., RA Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., RA Whitehead S., Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL111168; CAL35047.1; -; Genomic_DNA. DR PIR; F81366; F81366. DR RefSeq; WP_002853297.1; NC_002163.1. DR RefSeq; YP_002344325.1; NC_002163.1. DR ProteinModelPortal; Q9PP06; -. DR IntAct; Q9PP06; 13. DR STRING; 192222.Cj0927; -. DR PaxDb; Q9PP06; -. DR EnsemblBacteria; CAL35047; CAL35047; Cj0927. DR GeneID; 905205; -. DR KEGG; cje:Cj0927; -. DR PATRIC; 20058798; VBICamJej33762_0911. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CJEJ192222:GJTS-895-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000799; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 182 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149368. SQ SEQUENCE 182 AA; 20671 MW; 96C575308263D94A CRC64; MIKLTQEEQK YLLDSIRIIP DFPKKGIIFR DITTLLNNKE ALNFLLKHLK ERYKDYNLDF IAGTESRGFI FASMICAKLN LPFVPIRKPG KLPFETFSCE YDLEYGSDKV ELHKDAFKNI QNARVLLVDD LIATGGTAIA SYELIQKAGA KCVEACFLIN LKDLNGANKL EKLTSVYSVL EI // ID APT_CHLL7 Reviewed; 177 AA. AC Q3B250; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Plut_1727; OS Chlorobium luteolum (strain DSM 273 / 2530) (Pelodictyon luteolum). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Pelodictyon. OX NCBI_TaxID=319225; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 273 / 2530; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Pelodictyon luteolum DSM 273."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000096; ABB24581.1; -; Genomic_DNA. DR RefSeq; WP_011358453.1; NC_007512.1. DR ProteinModelPortal; Q3B250; -. DR STRING; 319225.Plut_1727; -. DR EnsemblBacteria; ABB24581; ABB24581; Plut_1727. DR KEGG; plt:Plut_1727; -. DR PATRIC; 21381108; VBIChlLut1287_1811. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; PLUT319225:GHDM-1733-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002709; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 177 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000319. SQ SEQUENCE 177 AA; 19121 MW; AABA972C1CA95AC3 CRC64; MPIKSRIRAI PDYPKKGIMF RDITTLIKDP VGFRLVIDNL TQRYLENGVD FDVIVGIEAR GFIIGSALAY ALGKGFVPVR KPGKLPADTV SQEYALEYGT DKIEIHIDAL EKGARVLLVD DLLATGGTAL AAAPLIEKVG GVVSEMAFIV NLPDIGGEEK ILAKGYKVFS LTAFEGE // ID APT_CALBD Reviewed; 175 AA. AC B9ML31; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 11-NOV-2015, entry version 46. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Athe_1952; OS Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) OS (Anaerocellum thermophilum). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=521460; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Kataeva I., Adams M.W.W.; RT "Complete sequence of chromosome of Anaerocellum thermophilum DSM RT 6725."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001393; ACM61039.1; -; Genomic_DNA. DR RefSeq; WP_013429776.1; NC_012034.1. DR ProteinModelPortal; B9ML31; -. DR STRING; 521460.Athe_1952; -. DR EnsemblBacteria; ACM61039; ACM61039; Athe_1952. DR KEGG; ate:Athe_1952; -. DR PATRIC; 20901104; VBIAnaThe135187_2045. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CBES521460:GH8H-1991-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000007723; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 175 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116227. SQ SEQUENCE 175 AA; 19495 MW; 209F3CFF861891D5 CRC64; MNLKEKFRHV LNFPKEGIDF IDITTVLQDK DAFKYAIDSL VNLVKDLDFE LIVGPESRGF IFGAPVAYVL NKGLVLVRKK GKLPYKTVSV EYELEYGKDV LEMHIDAIKP GQKVVIIDDL LATGGTTLSN IKLVEKLGGE VVGIAYLVEL TYLGGRENLK GYDVRSVVQF ESSLI // ID APT_CLAMS Reviewed; 191 AA. AC B0RGV9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 09-DEC-2015, entry version 52. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=CMS1178; OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM OS 20744 / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum). OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Clavibacter. OX NCBI_TaxID=31964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1; RX PubMed=18192393; DOI=10.1128/JB.01598-07; RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., RA Parkhill J., Ishimaru C.A.; RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis RT subsp. sepedonicus suggests recent niche adaptation."; RL J. Bacteriol. 190:2150-2160(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM849034; CAQ01293.1; -; Genomic_DNA. DR RefSeq; WP_012298573.1; NC_010407.1. DR ProteinModelPortal; B0RGV9; -. DR STRING; 31964.CMS_1178; -. DR EnsemblBacteria; CAQ01293; CAQ01293; CMS1178. DR KEGG; cms:CMS1178; -. DR PATRIC; 21459352; VBIClaMic4666_1238. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR KO; K00759; -. DR OMA; EDPRING; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CMIC31964:GJBN-1186-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001318; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 191 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000334711. SQ SEQUENCE 191 AA; 19782 MW; 19589FC8F96559CA CRC64; MRLTDRRRPA TDYRCRVPET SASDLVRSLL LTVPDFPQPG ILFRDLTPVL ADGAGLRAVV DNLVAAGGPV DAVAGVEARG FLLAAAAAYA SGVGTLAVRK AGKLPGEVLR ETYALEYGEA AIELHPGQLA PGSRVLLLDD VLATGGTLEA AARLLERAGY EVAGIGVVLE LADLGGRARL AGHDVHAILS L // ID APT_CAMJJ Reviewed; 182 AA. AC A1VZR0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CJJ81176_0934; OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=354242; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=81-176; RA Fouts D.E., Nelson K.E., Sebastian Y.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000538; EAQ71886.1; -; Genomic_DNA. DR RefSeq; WP_002855863.1; NZ_AASL01000001.1. DR ProteinModelPortal; A1VZR0; -. DR STRING; 354242.Cjejjejuni_010100004835; -. DR EnsemblBacteria; EAQ71886; EAQ71886; CJJ81176_0934. DR KEGG; cjj:CJJ81176_0934; -. DR PATRIC; 20051835; VBICamJej103413_0939. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CJEJ354242:GC51-908-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000646; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 182 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000271. SQ SEQUENCE 182 AA; 20723 MW; FDE95D9793A15B45 CRC64; MIKLTQEEQK YLFDSIRIIP DFPKKGIIFR DITTLLNNKE ALNFLLKHLK ERYKDYNLDF IAGTESRGFI FASMICAKLN LPFVPIRKPG KLPFETFSCE YDLEYGSDKV ELHKDAFKNI QNARVLLVDD LIATGGTAIA SYELIQKAGA KCVEACFLMN LKDLNGANKL EKLTSVYSVL EI // ID APT_CAMJD Reviewed; 182 AA. AC A7H3C4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=JJD26997_0887; OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / OS 269.97). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., Lastovica A.J., Nelson K.E.; RT "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 RT isolated from human blood."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000768; ABS43878.1; -; Genomic_DNA. DR RefSeq; WP_002865899.1; NC_009707.1. DR ProteinModelPortal; A7H3C4; -. DR EnsemblBacteria; ABS43878; ABS43878; JJD26997_0887. DR KEGG; cjd:JJD26997_0887; -. DR PATRIC; 20047435; VBICamJej122183_0889. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CJEJ360109:GJDG-855-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002302; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 182 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000270. SQ SEQUENCE 182 AA; 20689 MW; C68175308263D94D CRC64; MIKLTQEEQK YLLDSIRIIP DFPKKGIIFR DITTLLNNKE ALNFLLKHLK ERYKDYNLDF IAGTESRGFI FASMICAKLN LPFVPIRKPG KLPFETFSCE YDLEYGSDKV ELHKDAFKNI QNARVLLVDD LIATGGTAIA SYELIQKAGA KCVEACFLMN LKDLNGANKL EKLTSVYSVL EI // ID APT_CLOAB Reviewed; 172 AA. AC Q97GU0; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CA_C2275; OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG OS 5710 / VKM B-1787). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., RA Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., RA Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., RA Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE001437; AAK80232.1; -; Genomic_DNA. DR PIR; E97180; E97180. DR RefSeq; NP_348892.1; NC_003030.1. DR RefSeq; WP_010965573.1; NC_003030.1. DR ProteinModelPortal; Q97GU0; -. DR STRING; 272562.CA_C2275; -. DR EnsemblBacteria; AAK80232; AAK80232; CA_C2275. DR GeneID; 1118458; -. DR KEGG; cac:CA_C2275; -. DR PATRIC; 32038921; VBICloAce74127_2473. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CACE272562:GJIH-2324-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000814; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149373. SQ SEQUENCE 172 AA; 18855 MW; F6B72B0EE32FE631 CRC64; MDLKDSIRVI DGFPKEGISF KDVTTLIQDK EAYKYSVDKI GEYLKDKNVD LIVAPEARGF LFGAPVAYKI GAGFIPVRKK GKLPCETVEV TYELEYGEDI LEMHKDAIKK GQRVAIVDDL LATGGTINSV AKLVEALGGE VVAACFVVEL TDLNGKDKLG DYDTMSLVKY NV // ID APT_CHLP8 Reviewed; 177 AA. AC B3QQD1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 11-NOV-2015, entry version 49. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Cpar_1742; OS Chlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. OS thiosulfatophilum (strain DSM 263 / NCIB 8327)). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=517417; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCIB 8327; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., RA Liu Z., Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobaculum parvum NCIB 8327."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001099; ACF12134.1; -; Genomic_DNA. DR RefSeq; WP_012502967.1; NC_011027.1. DR ProteinModelPortal; B3QQD1; -. DR STRING; 517417.Cpar_1742; -. DR EnsemblBacteria; ACF12134; ACF12134; Cpar_1742. DR KEGG; cpc:Cpar_1742; -. DR PATRIC; 21366785; VBIChlPar72705_1744. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CPAR517417:GH95-1786-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000008811; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 177 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088962. SQ SEQUENCE 177 AA; 19245 MW; 7999BFA45D477DCE CRC64; MPIKSRIRTV PDYPKKGIMF RDITTLIKDP VGFRLVIDNM TQHYLSNGID FDVIVGIEAR GFIIGGALSY TLGKGFVPVR KPGKLPADVV QLEYDLEYGS DKIEMHTDSL VKGQRVLLVD DLLATGGTAL AAAALVEKLG GVVASMGFIV NLPDVGGEKK IRDKGYNIFS LTEFEGD // ID APT_CALS8 Reviewed; 175 AA. AC A4XI79; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Csac_1000; OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / OS Tp8T 6331). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family III. Incertae Sedis; OC Caldicellulosiruptor. OX NCBI_TaxID=351627; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., RA van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., RA Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., RA Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., RA Richardson P.; RT "Genome sequence of the thermophilic hydrogen-producing bacterium RT Caldicellulosiruptor saccharolyticus DSM 8903."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000679; ABP66614.1; -; Genomic_DNA. DR RefSeq; WP_011916560.1; NC_009437.1. DR ProteinModelPortal; A4XI79; -. DR STRING; 351627.Csac_1000; -. DR EnsemblBacteria; ABP66614; ABP66614; Csac_1000. DR KEGG; csc:Csac_1000; -. DR PATRIC; 21251630; VBICalSac56748_1131. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CSAC351627:GJ17-1027-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000256; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 175 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000265. SQ SEQUENCE 175 AA; 19551 MW; CC4F291BCF2BEC7F CRC64; MNLKEKFRHV LNFPKEGIDF IDITTVLQDK DAFKYAIDSL VNLVKDLDFD LIVGPESRGF IFGAPVAYVL NKGLVLVRKK GKLPYKTVSV EYELEYGKDI LEMHIDAIQP GQKVVIIDDL LATGGTTLSN IKLVEKLGGK VVGIAYLVEL TYLNGRENLK GYDVRSVVQF ESSLI // ID APT_CLOCE Reviewed; 171 AA. AC B8I3F7; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 11-NOV-2015, entry version 46. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Ccel_1952; OS Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / OS H10). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=394503; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., RA Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Kyrpides N., Ivanova N., Zhou J., Richardson P.; RT "Complete sequence of Clostridium cellulolyticum H10."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001348; ACL76300.1; -; Genomic_DNA. DR RefSeq; WP_015925404.1; NC_011898.1. DR ProteinModelPortal; B8I3F7; -. DR STRING; 394503.Ccel_1952; -. DR EnsemblBacteria; ACL76300; ACL76300; Ccel_1952. DR KEGG; cce:Ccel_1952; -. DR PATRIC; 19434811; VBICloCel57783_2008. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CCEL394503:GJET-1997-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001349; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 171 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116235. SQ SEQUENCE 171 AA; 19277 MW; 74E9F1B47719BDA3 CRC64; MDLKDKLRHV MDFPKEGIDF IDITTVLQDP EAFRECMESF KTLAEKMGDF DLIVGSESRG FIFGAPLAYR MEKGFVPVRK KGKLPYKTVR EEYDLEYGKD ELEIHSDAIA PGEKVLIVDD LLATGGTTEA NIKLVEKLGG EVTGIVYFIE LMSLKGRDKL KGYNVDSIVK F // ID APT_CLAM3 Reviewed; 175 AA. AC A5CSP7; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CMM_2055; OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382). OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; OC Clavibacter. OX NCBI_TaxID=443906; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 382; RX PubMed=18192381; DOI=10.1128/JB.01595-07; RA Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., RA Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., RA Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., RA Rueckert C., Schneiker S., Zellermann E.-M., Puehler A., RA Eichenlaub R., Kaiser O., Bartels D.; RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter RT michiganensis subsp. michiganensis NCPPB382 reveals a large island RT involved in pathogenicity."; RL J. Bacteriol. 190:2138-2149(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM711867; CAN02118.1; -; Genomic_DNA. DR RefSeq; WP_012038742.1; NC_009480.1. DR ProteinModelPortal; A5CSP7; -. DR STRING; 443906.CMM_2055; -. DR EnsemblBacteria; CAN02118; CAN02118; CMM_2055. DR KEGG; cmi:CMM_2055; -. DR PATRIC; 21454937; VBIClaMic82482_2174. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CMIC443906:GCI2-2117-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001564; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 175 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321356. SQ SEQUENCE 175 AA; 17954 MW; 56AADDD9EFC645D9 CRC64; MPETPASDLV RSLLLTVPDF PQPGILFRDL TPVLADGPAL RAVVDDLVAA CGPVDAVAGV EARGFLLAAA AAYASGVGTL AVRKAGKLPG EVLRETYALE YGEAAIELHP GQLAPGSRVL LLDDVLATGG TLEAAARLLE RAGYEVAGIG VVLELADLGG RERLAGHDVR AILTL // ID APT_CLOPE Reviewed; 172 AA. AC Q8XJ22; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=CPE1939; OS Clostridium perfringens (strain 13 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195102; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=13 / Type A; RX PubMed=11792842; DOI=10.1073/pnas.022493799; RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., RA Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.; RT "Complete genome sequence of Clostridium perfringens, an anaerobic RT flesh-eater."; RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000016; BAB81645.1; -; Genomic_DNA. DR RefSeq; WP_003451591.1; NC_003366.1. DR ProteinModelPortal; Q8XJ22; -. DR EnsemblBacteria; BAB81645; BAB81645; BAB81645. DR GeneID; 990253; -. DR KEGG; cpe:CPE1939; -. DR PATRIC; 19497841; VBICloPer59675_2011. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CPER195102:GJFM-1992-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000818; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149374. SQ SEQUENCE 172 AA; 18602 MW; 45938D903A9E3C7E CRC64; MSLKDKIRVI EDFPKKGISF KDITTLIADG EGLRDSVDQM AEFFKDKNID VVVGPEARGF IFGVPVAYAL GVGFIPVRKP GKLPGDTVRV EYDLEYGKDA LEIHKDAIKP GMRVAIVDDL LATGGTIAAV AKLVEQAGGE VAGLAFTIEL TELKGRDKLK GYEVTSLVDY DV // ID APT_CUPMC Reviewed; 190 AA. AC Q1LRM9; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Rmet_0311; OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 OS / CH34) (Ralstonia metallidurans). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=266264; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Mergeay M., Benotmane M.A., RA Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., RA van der Lelie D., Richardson P.; RT "Complete sequence of the chromosome of Ralstonia metallidurans RT CH34."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000352; ABF07197.1; -; Genomic_DNA. DR RefSeq; WP_011515197.1; NC_007973.1. DR ProteinModelPortal; Q1LRM9; -. DR STRING; 266264.Rmet_0311; -. DR EnsemblBacteria; ABF07197; ABF07197; Rmet_0311. DR GeneID; 24150654; -. DR KEGG; rme:Rmet_0311; -. DR PATRIC; 20285160; VBIRalMet4734_0695. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CMET266264:GJ5G-321-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002429; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 190 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321390. SQ SEQUENCE 190 AA; 20740 MW; 003A75CC0F8465CE CRC64; MSNSIIQSPD LGDVTGYLRD RIRTVPDWPQ PGVMFRDITP LLQNPKTLRV LIDVFVHRYM DQNLDLVAGI DARGFILGSI IAYELNLGFV PIRKKGKLPF QTVAEEYELE YGSATVEIHA DACKPGDRVL LIDDLIATGG TMMAGRKLLE RLGATVVEGG AIVDLPELGG SKLLQASGLS LFTVCNFDGH // ID APT_CHESB Reviewed; 181 AA. AC Q11GC0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Meso_2163; OS Chelativorans sp. (strain BNC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Chelativorans. OX NCBI_TaxID=266779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BNC1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P.; RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000390; ABG63555.1; -; Genomic_DNA. DR RefSeq; WP_011581497.1; NC_008254.1. DR ProteinModelPortal; Q11GC0; -. DR SMR; Q11GC0; 9-181. DR STRING; 266779.Meso_2163; -. DR EnsemblBacteria; ABG63555; ABG63555; Meso_2163. DR KEGG; mes:Meso_2163; -. DR PATRIC; 21344464; VBICheSp72577_2853. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CSP266779:GI09-2200-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001820; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 181 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000305. SQ SEQUENCE 181 AA; 19544 MW; 6E20BBFD2F638115 CRC64; MKQSLEDTLL AAIRTIPDYP RPGILFRDIT TLLGDARAFR RAVDELVHPY AGAKIDKIAG IEARGFILGG AIAHQLSSGF IPIRKKGKLP HETVRVAYSL EYGLDEMEMH IDAVSPGEKV ILVDDLIATG GTAEAAVRLL RQMGAEIVAA CFVIDLPDLG GRAKLEAEGV DVRTLVSFEG H // ID APT_CANAL Reviewed; 188 AA. AC Q5ALX8; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 20-JAN-2016, entry version 69. DE RecName: Full=Adenine phosphoribosyltransferase; DE Short=APRT; DE EC=2.4.2.7; GN Name=APT1; ORFNames=CaO19.1448, CaO19.9023; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; OC Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., RA Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., RA Davis R.W., Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACQ01000008; EAL03604.1; -; Genomic_DNA. DR EMBL; AACQ01000007; EAL03751.1; -; Genomic_DNA. DR RefSeq; XP_722359.1; XM_717266.1. DR RefSeq; XP_722498.1; XM_717405.1. DR ProteinModelPortal; Q5ALX8; -. DR SMR; Q5ALX8; 6-179. DR EnsemblFungi; EAL03604; EAL03604; CaO19.9023. DR EnsemblFungi; EAL03751; EAL03751; CaO19.1448. DR GeneID; 3635842; -. DR GeneID; 3635988; -. DR KEGG; cal:CaO19.1448; -. DR KEGG; cal:CaO19.9023; -. DR CGD; CAL0000192887; APT1. DR InParanoid; Q5ALX8; -. DR KO; K00759; -. DR OrthoDB; EOG7WT4CC; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000559; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006168; P:adenine salvage; IEA:InterPro. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Magnesium; KW Metal-binding; Nucleus; Purine salvage; Reference proteome; KW Transferase. FT CHAIN 1 188 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000227899. FT NP_BIND 134 138 AMP. {ECO:0000250}. SQ SEQUENCE 188 AA; 20877 MW; 8CA335A0D1F675F6 CRC64; MSDRVLEINA LAKELKANLK QFPNFPKEGI LFEDFLPIFT KPDLFNKLVK AFKLHVGEQK IDYVIGLESR GFLFGPTLAL ALNAGFVPVR KPGKLPGPTF KVEFQKEYGS DEFEIQQDVI PKGAKVLIVD DILATGGSAF GAGELAKKTG AEIVEYLFVM ELDFLKGRDK LDAPVYTLFG GQEEKFTE // ID APT_COPPD Reviewed; 175 AA. AC B5Y8Y0; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 11-NOV-2015, entry version 51. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=COPRO5265_0896; OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermodesulfobiaceae; Coprothermobacter. OX NCBI_TaxID=309798; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35245 / DSM 5265 / BT; RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.; RT "The complete genome sequence of Coprothermobacter proteolyticus RT strain ATCC 5245 / DSM 5265 / BT."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001145; ACI17626.1; -; Genomic_DNA. DR RefSeq; WP_012544278.1; NC_011295.1. DR ProteinModelPortal; B5Y8Y0; -. DR STRING; 309798.COPRO5265_0896; -. DR EnsemblBacteria; ACI17626; ACI17626; COPRO5265_0896. DR KEGG; cpo:COPRO5265_0896; -. DR PATRIC; 21474620; VBICopPro72829_0837. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CPRO309798:GH7M-889-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001732; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 175 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116168. SQ SEQUENCE 175 AA; 18979 MW; 81DE520ADFD8B61E CRC64; MRVDDLRQYI RDIPNFPTEG VIFRDITPLL KNPDAFATTV DLMAEAVSSL NVTAVAAVEA RGFIWGGTLA YRLGVGFIPI RKPGKLPFEV VEKEFELEYG KDVLQIHKDA AGPGDSILIV DDVLATGGTA QAAADLVNTL GADVAGFCFL LRLGTMDGYE RLSKLGKKVF YLLTV // ID APT_CROS8 Reviewed; 183 AA. AC A7MJV7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=ESA_02801; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894; RX PubMed=20221447; DOI=10.1371/journal.pone.0009556; RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., RA Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., RA Wilson R.K., McClelland M., Forsythe S.J.; RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative RT genomic hybridization analysis with other Cronobacter species."; RL PLoS ONE 5:E9556-E9556(2010). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000783; ABU78031.1; -; Genomic_DNA. DR RefSeq; WP_004386902.1; NC_009778.1. DR ProteinModelPortal; A7MJV7; -. DR SMR; A7MJV7; 2-183. DR STRING; 290339.ESA_02801; -. DR EnsemblBacteria; ABU78031; ABU78031; ESA_02801. DR GeneID; 5552297; -. DR KEGG; esa:ESA_02801; -. DR PATRIC; 20397445; VBICroSak107175_2494. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CSAK290339:GJ80-2791-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000260; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 183 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000281. SQ SEQUENCE 183 AA; 20002 MW; E9F52A8119FA506E CRC64; MTATAQQLEY LKNSIKSIQD YPKPGILFRD VTSLLEDPKA YALSIELLVE RYKNAGITKV VGTEARGFLF GAPVALALGV GFVPVRKPRK LPRETIAESY ELEYGTDQLE IHVDAIKPGD KVLVVDDLLA TGGTIEATVK LIRRLGGEVT DAAFIINLFD IGGEERLNKQ GITCYSLVPF PGH // ID APT_CLOK1 Reviewed; 172 AA. AC B9E5P8; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 11-NOV-2015, entry version 46. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CKR_2772; OS Clostridium kluyveri (strain NBRC 12016). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=583346; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 12016; RA Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., RA Vertes A.A., Yukawa H.; RT "Complete genome sequence of Clostridium kluyveri and comparative RT genomics of Clostridia species."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009049; BAH07823.1; -; Genomic_DNA. DR RefSeq; WP_012103475.1; NC_011837.1. DR ProteinModelPortal; B9E5P8; -. DR EnsemblBacteria; BAH07823; BAH07823; CKR_2772. DR KEGG; ckr:CKR_2772; -. DR PATRIC; 19475783; VBICloKlu118830_3134. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CKLU583346:GJNQ-2821-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000007969; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116236. SQ SEQUENCE 172 AA; 18928 MW; E94F38197E4A96DF CRC64; MNLQDNIRIV EGFPKKGISF KDITTLIRDK DAFKYAVDKI AGYLKDKNID VVVGPEARGF LFGAPIAYTL GAGFVPVRKQ GKLPYDTLSI KYDLEYGSDV LQIHKDAINK GDRVALVDDL LATGGTTSSV VKLIEQAGGE IVTIDFVIEL TDLKGREKLK GYDVLSLIKY DI // ID APT_CLOPH Reviewed; 174 AA. AC A9KIA0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Cphy_0547; OS Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OS (Lachnoclostridium phytofermentans). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=357809; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700394 / DSM 18823 / ISDg; RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., RA Brettin T., Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P.; RT "Complete genome sequence of Clostridium phytofermentans ISDg."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000885; ABX40934.1; -; Genomic_DNA. DR RefSeq; WP_012198578.1; NC_010001.1. DR ProteinModelPortal; A9KIA0; -. DR STRING; 357809.Cphy_0547; -. DR EnsemblBacteria; ABX40934; ABX40934; Cphy_0547. DR KEGG; cpy:Cphy_0547; -. DR PATRIC; 19500642; VBICloPhy16213_0563. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CPHY357809:GHCL-590-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000370; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 174 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000073790. SQ SEQUENCE 174 AA; 19418 MW; 0AF928B39F897AE7 CRC64; MKKLEEYVRS IPDFPEEGII FRDVTSVLQD KDSLKMSIDQ MQENLNGLDF DVIVGPESRG FIFGVPIAYN LNKAFIPVRK KGKLPCETVE MEYALEYGTA TIEMHKDSIK PGQKVVIIDD LIATGGTIEA ITKLIEQLGG EVVKIVFLME LEGLMGREKL KGYDIASVIK YAGK // ID APT4_ARATH Reviewed; 182 AA. AC Q9SU38; DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 20-JAN-2016, entry version 121. DE RecName: Full=Adenine phosphoribosyltransferase 4; DE Short=AtAPT4; DE EC=2.4.2.7; GN Name=APT4; OrderedLocusNames=At4g12440; ORFNames=T1P17.30; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M.A., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE. RX PubMed=23658065; DOI=10.1093/mp/sst071; RA Zhang X., Chen Y., Lin X., Hong X., Zhu Y., Li W., He W., An F., RA Guo H.; RT "Adenine phosphoribosyl transferase 1 is a key enzyme catalyzing RT cytokinin conversion from nucleobases to nucleotides in Arabidopsis."; RL Mol. Plant 6:1661-1672(2013). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC May contribute to the recycling of adenine into adenylate CC nucleotides and the inactivation of cytokinins by CC phosphoribosylation. Possesses low activity toward adenine, but CC can efficiently convert cytokinins from free bases (active form) CC to the corresponding nucleotides (inactive form). CC {ECO:0000269|PubMed:23658065}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000269|PubMed:23658065}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q9SU38-1; Sequence=Displayed; CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth CC conditions. {ECO:0000269|PubMed:23658065}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AL049730; CAB41714.1; -; Genomic_DNA. DR EMBL; AL161534; CAB78287.1; -; Genomic_DNA. DR EMBL; CP002687; AEE83133.1; -; Genomic_DNA. DR EMBL; AY133689; AAM91623.1; -; mRNA. DR PIR; T07636; T07636. DR RefSeq; NP_192981.1; NM_117314.2. [Q9SU38-1] DR UniGene; At.33474; -. DR ProteinModelPortal; Q9SU38; -. DR SMR; Q9SU38; 10-181. DR STRING; 3702.AT4G12440.2; -. DR iPTMnet; Q9SU38; -. DR PaxDb; Q9SU38; -. DR PRIDE; Q9SU38; -. DR EnsemblPlants; AT4G12440.2; AT4G12440.2; AT4G12440. [Q9SU38-1] DR GeneID; 826856; -. DR KEGG; ath:AT4G12440; -. DR TAIR; AT4G12440; -. DR eggNOG; KOG1712; Eukaryota. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR InParanoid; Q9SU38; -. DR KO; K00759; -. DR OMA; RYIRNIP; -. DR PhylomeDB; Q9SU38; -. DR BioCyc; ARA:AT4G12440-MONOMER; -. DR Reactome; R-ATH-74217; Purine salvage. DR UniPathway; UPA00588; UER00646. DR PRO; PR:Q9SU38; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q9SU38; baseline and differential. DR Genevisible; Q9SU38; AT. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IDA:UniProtKB. DR GO; GO:0006168; P:adenine salvage; IEA:InterPro. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Cytoplasm; KW Glycosyltransferase; Purine salvage; Reference proteome; Transferase. FT CHAIN 1 182 Adenine phosphoribosyltransferase 4. FT /FTId=PRO_0000430131. SQ SEQUENCE 182 AA; 20355 MW; 976CA5085032935B CRC64; MSENEVKDPR IDGIKTKIRV VPDFPKKGIM FQDITTLLLD PKAFKDTIDL FVERYRDMNI SVVAGIEARG FIFGSPIALA IGAKFVPLRK PKKLPGQIIF EEYELEYGSD RLEMHVEAVD SGDRALVVDD LIATGGTLCA AMNLLKRVGA EVIECACVIE LPELKGRERL EGKPLYVLVE YR // ID APT_BACAH Reviewed; 170 AA. AC A0RJ16; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BALH_3989; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=412694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam; RX PubMed=17337577; DOI=10.1128/JB.00241-07; RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P., RA Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., RA Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., RA Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., RA Wills P.L., Gilna P., Brettin T.S.; RT "The complete genome sequence of Bacillus thuringiensis Al Hakam."; RL J. Bacteriol. 189:3680-3681(2007). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000485; ABK87209.1; -; Genomic_DNA. DR RefSeq; WP_000346214.1; NC_008600.1. DR ProteinModelPortal; A0RJ16; -. DR EnsemblBacteria; ABK87209; ABK87209; BALH_3989. DR KEGG; btl:BALH_3989; -. DR PATRIC; 19000863; VBIBacThu63319_4429. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BTHU412694:GH1W-3903-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000761; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000256. SQ SEQUENCE 170 AA; 18644 MW; 148BA98F47CF8FFC CRC64; MDFKQHIAIV PDYPKEGIVF KDITPLMNDG KAYKAATDAI VEYAKERDID LVVGPEARGF IIGCPVSYAL EVGFAPVRKL GKLPREVITV DYGKEYGKDV LTIHKDAIKP GQRVLITDDL LATGGTIEAT IKLVEELGGV VAGIAFLVEL TYLDGRKMLD GYDVLVLEKY // ID APT_ANAD2 Reviewed; 172 AA. AC B8JDQ9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 11-NOV-2015, entry version 43. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=A2cp1_0802; OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=455488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-1 / ATCC BAA-258; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Beliaev A.S., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001359; ACL64154.1; -; Genomic_DNA. DR RefSeq; WP_012524861.1; NC_011891.1. DR ProteinModelPortal; B8JDQ9; -. DR EnsemblBacteria; ACL64154; ACL64154; A2cp1_0802. DR KEGG; acp:A2cp1_0802; -. DR PATRIC; 20908456; VBIAnaDeh28364_0830. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; ADEH455488:GH35-807-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000007089; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116226. SQ SEQUENCE 172 AA; 18744 MW; 21DCC5D557590F90 CRC64; MMDAVRARIR DVPDFPKKGI VFKDITPVLS DPHTFREVID AFVERWKGER VDKVIGIESR GFIFAAPIAY ALGAGFTIVR KPGKLPWETI REVYALEYGE GALELHIDAI GPGDRVLVVD DVLATGGTAG AAGRLVVRQG AELLGYAFLA ELSFLNGARQ LGHAKVHSLL TF // ID APT_ANADF Reviewed; 177 AA. AC A7H8F4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Anae109_0788; OS Anaeromyxobacter sp. (strain Fw109-5). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=404589; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fw109-5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Fields M., Richardson P.; RT "Complete sequence of Anaeromyxobacter sp. Fw109-5."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000769; ABS25000.1; -; Genomic_DNA. DR ProteinModelPortal; A7H8F4; -. DR STRING; 404589.Anae109_0788; -. DR EnsemblBacteria; ABS25000; ABS25000; Anae109_0788. DR KEGG; afw:Anae109_0788; -. DR PATRIC; 20926701; VBIAnaSp113478_0835. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; ASP404589:GHMT-793-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000006382; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 177 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321335. SQ SEQUENCE 177 AA; 19298 MW; E20B6069D5E4831B CRC64; MVMSAAMEAV RARIRDVPDF PQKGIVFKDI TPVLADPTTF REVIDAFVAR WKDERISKVV GIESRGFLFA APLAYALGAG LTIARKPGKL PWETIREVYS LEYGENSLEL HIDAVKAGER VLVVDDVLAT GGTADAVGRL VTRQGATLVA YSFLVELGFL GGAKRLGREH VHALLSY // ID APT_BACCN Reviewed; 170 AA. AC A7GT90; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 16-MAR-2016, entry version 62. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Bcer98_3124; OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH OS 391-98). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=315749; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98; RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003; RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., RA Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., RA Weissenbach J., Ehrlich S.D., Sorokin A.; RT "Extending the Bacillus cereus group genomics to putative food-borne RT pathogens of different toxicity."; RL Chem. Biol. Interact. 171:236-249(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000764; ABS23348.1; -; Genomic_DNA. DR RefSeq; WP_012095585.1; NC_009674.1. DR ProteinModelPortal; A7GT90; -. DR STRING; 315749.Bcer98_3124; -. DR EnsemblBacteria; ABS23348; ABS23348; Bcer98_3124. DR KEGG; bcy:Bcer98_3124; -. DR PATRIC; 18934880; VBIBacCyt128034_3283. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BCYT315749:GH2A-3232-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002300; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000073787. SQ SEQUENCE 170 AA; 18723 MW; E3BAB44E4FF940B0 CRC64; MDFKQHIAIV PDYPKEGIVF KDITPLMNNG KAYKAATDEI VAYAKERNID LVVGPEARGF IIGCPVSYAL EVGFAPVRKL GKLPREIIKV DYGKEYGKDV LTIHKDAIKP GQRVLITDDL LATGGTIEAT IQLVEELGGI VAGIAFLVEL TYLEGREKLE GYDVLVLEKY // ID APT_BACFN Reviewed; 178 AA. AC Q5LIY6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=BF0112; OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC OS 9343). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=272559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343; RX PubMed=15746427; DOI=10.1126/science.1107008; RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., RA Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., RA Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., RA Line A., Lord A., Norbertczak H., Ormond D., Price C., RA Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J.; RT "Extensive DNA inversions in the B. fragilis genome control variable RT gene expression."; RL Science 307:1463-1465(2005). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR626927; CAH05890.1; -; Genomic_DNA. DR ProteinModelPortal; Q5LIY6; -. DR STRING; 272559.BF0112; -. DR EnsemblBacteria; CAH05890; CAH05890; BF9343_0111. DR KEGG; bfs:BF9343_0111; -. DR PATRIC; 21036684; VBIBacFra29119_0108. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BFRA272559:GKF0-112-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000006731; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 178 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000257. SQ SEQUENCE 178 AA; 20134 MW; 96EE31B2EC81824D CRC64; MIMSKEKLIK SIREVPDFPI PGILFYDVTT LFKDSERLQE LSDIMYEMYK DKGITKVVGI ESRGFIMGPI LATRLGAGFI PIRKPGKLPA ETMEESYDKE YGKDTVQIHK DALNENDVVL LHDDLLATGG TMKAACNLVK KLHPKKVYVN FIIELKELNG KQVFENDQDV DIQSVLSL // ID APT_BACV8 Reviewed; 174 AA. AC A6KZN9; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 17-FEB-2016, entry version 60. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BVU_1213; OS Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / NBRC OS 14291 / NCTC 11154). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=435590; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / NBRC 14291 / NCTC 11154; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., RA Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., RA Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., RA Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(2007). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000139; ABR38903.1; -; Genomic_DNA. DR RefSeq; WP_005843916.1; NC_009614.1. DR ProteinModelPortal; A6KZN9; -. DR STRING; 435590.BVU_1213; -. DR EnsemblBacteria; ABR38903; ABR38903; BVU_1213. DR GeneID; 5302179; -. DR KEGG; bvu:BVU_1213; -. DR PATRIC; 21067254; VBIBacVul85104_1261. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BVUL435590:GH96-1210-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002861; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 174 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321339. SQ SEQUENCE 174 AA; 19188 MW; 40FB9A8686EA869F CRC64; MSKETLKANL REIPDFPIPG ILFYDVTTLF KNPECLQEIL DTLYEMYKDK GITKVVGIES RGFIMGGALA ARLGAGFVMA RKPGKLPAEV VEETYAKEYG TDTIQIHKDA IDENDVVLLH DDLLATGGTM AATHRLVQRC GAKKIFINFI IELGGLNGRK AFPEDITVDT LLTL // ID APT_BACMF Reviewed; 170 AA. AC A7Z756; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=RBAM_024720; OS Bacillus methylotrophicus (strain DSM 23117 / BGSC 10A6 / FZB42) OS (Bacillus amyloliquefaciens subsp. plantarum). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=326423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23117 / BGSC 10A6 / FZB42; RX PubMed=17704766; DOI=10.1038/nbt1325; RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., RA Strittmatter A., Gottschalk G., Borriss R.; RT "Comparative analysis of the complete genome sequence of the plant RT growth-promoting bacterium Bacillus amyloliquefaciens FZB42."; RL Nat. Biotechnol. 25:1007-1014(2007). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000560; ABS74832.1; -; Genomic_DNA. DR RefSeq; WP_003152714.1; NC_009725.1. DR ProteinModelPortal; A7Z756; -. DR STRING; 326423.RBAM_024720; -. DR EnsemblBacteria; ABS74832; ABS74832; RBAM_024720. DR KEGG; bay:RBAM_024720; -. DR PATRIC; 18750056; VBIBacAmy31356_2503. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BAMY326423:GCM4-2470-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001120; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000255. SQ SEQUENCE 170 AA; 18848 MW; DB42A69B8D1CBDFA CRC64; MDLKKYVTIV PDYPKEGVQF KDITTLMDKG DVYRYATDQI VEYAKEKEID LVVGPEARGF IIGCPVAYAL GVGFAPVRKE GKLPREVIKV DYGLEYGKDV LTIHKDAILP GQRVLITDDL LATGGTIEAT IKLVEELGGV VAGIAFLIEL SYLDGRDKLD DYDILTLMKY // ID APT_BOVIN Reviewed; 180 AA. AC Q56JW4; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 17-FEB-2016, entry version 83. DE RecName: Full=Adenine phosphoribosyltransferase; DE Short=APRT; DE EC=2.4.2.7; GN Name=APRT; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymphoid epithelium; RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.; RT "Analysis of sequences obtained from constructed full-length bovine RT cDNA libraries."; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY911367; AAW82131.1; -; mRNA. DR EMBL; BC102283; AAI02284.1; -; mRNA. DR RefSeq; NP_001020505.1; NM_001025334.2. DR UniGene; Bt.6947; -. DR ProteinModelPortal; Q56JW4; -. DR SMR; Q56JW4; 2-180. DR STRING; 9913.ENSBTAP00000000841; -. DR PaxDb; Q56JW4; -. DR PRIDE; Q56JW4; -. DR Ensembl; ENSBTAT00000000841; ENSBTAP00000000841; ENSBTAG00000000639. DR GeneID; 519017; -. DR KEGG; bta:519017; -. DR CTD; 353; -. DR eggNOG; KOG1712; Eukaryota. DR eggNOG; COG0503; LUCA. DR GeneTree; ENSGT00390000017259; -. DR HOGENOM; HOG000036776; -. DR HOVERGEN; HBG003144; -. DR InParanoid; Q56JW4; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG7FFMT9; -. DR TreeFam; TF300227; -. DR Reactome; R-BTA-74217; Purine salvage. DR UniPathway; UPA00588; UER00646. DR NextBio; 20872789; -. DR Proteomes; UP000009136; Chromosome 18. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. DR GO; GO:0002055; F:adenine binding; IEA:Ensembl. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016208; F:AMP binding; IEA:Ensembl. DR GO; GO:0006168; P:adenine salvage; IEA:InterPro. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0007625; P:grooming behavior; IEA:Ensembl. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 2: Evidence at transcript level; KW Acetylation; Complete proteome; Cytoplasm; Glycosyltransferase; KW Phosphoprotein; Purine salvage; Reference proteome; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P07741}. FT CHAIN 2 180 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000240344. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000250|UniProtKB:P07741}. FT MOD_RES 15 15 Phosphoserine. FT {ECO:0000250|UniProtKB:P07741}. FT MOD_RES 30 30 Phosphoserine. FT {ECO:0000250|UniProtKB:P36972}. FT MOD_RES 60 60 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P07741}. FT MOD_RES 66 66 Phosphoserine. FT {ECO:0000250|UniProtKB:P07741}. FT MOD_RES 135 135 Phosphothreonine. FT {ECO:0000250|UniProtKB:P07741}. SQ SEQUENCE 180 AA; 19537 MW; 12594AF43DAFBCD4 CRC64; MADPELQLVA RRIRSFPNFP IPGVLFRDIS PVLKDPTSFR ASINLLANHL KKAHGGRIDY IAGLDSRGFL FGPSLAQELG LGCILIRKRG KLPGPTVCAS YALEYGKGEL EIQRDALEPG QKVVVVDDLL ATGGTMCAAC ELLGQLRAEV LECVSLVELT SLKGREKLGA VPFFSLLQYE // ID APT_ARTS2 Reviewed; 185 AA. AC A0JV33; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Arth_1509; OS Arthrobacter sp. (strain FB24). OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=290399; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FB24; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., RA Nakatsu C.H., Richardson P.; RT "Complete sequence of chromosome 1 of Arthrobacter sp. FB24."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000454; ABK02903.1; -; Genomic_DNA. DR RefSeq; WP_011691369.1; NC_008541.1. DR ProteinModelPortal; A0JV33; -. DR STRING; 290399.Arth_1509; -. DR EnsemblBacteria; ABK02903; ABK02903; Arth_1509. DR KEGG; art:Arth_1509; -. DR PATRIC; 20998315; VBIArtSp72239_1867. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; VHALCAF; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; ASP290399:GHIF-1541-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000754; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 185 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321337. SQ SEQUENCE 185 AA; 19450 MW; 06735EC3441AC0BD CRC64; MNQSEPGQTR RSVPVDQLIN SLCATVPDYP KPGIIFKDLT PVFANGAALR AVVDALVEPF KGQFDAVAGV EARGFLLAAA AAYATDTGVI TVRKAGKLPR KVISEDYALE YGTATLELHT ADLPAGSRVL ILDDVLATGG TLGAAARLFE RCGVHVAGVG VVMELGELRG RSALTGHRVR SLLRL // ID APT_BRUA1 Reviewed; 181 AA. AC B2S701; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BAbS19_I14550; OS Brucella abortus (strain S19). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=430066; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S19; RX PubMed=18478107; DOI=10.1371/journal.pone.0002193; RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., RA Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.; RT "Genome sequence of Brucella abortus vaccine strain S19 compared to RT virulent strains yields candidate virulence genes."; RL PLoS ONE 3:E2193-E2193(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000887; ACD72948.1; -; Genomic_DNA. DR RefSeq; WP_002964645.1; NC_010742.1. DR ProteinModelPortal; B2S701; -. DR SMR; B2S701; 8-181. DR STRING; 430066.BAbS19_I14550; -. DR PRIDE; B2S701; -. DR EnsemblBacteria; ACD72948; ACD72948; BAbS19_I14550. DR GeneID; 3788616; -. DR KEGG; bmc:BAbS19_I14550; -. DR PATRIC; 17820133; VBIBruAbo38055_2819. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BABO430066:GHI6-1449-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002565; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 181 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088955. SQ SEQUENCE 181 AA; 19614 MW; 128ABF9D88C2A953 CRC64; MESGFKVTLK DAIRTIPDYP KPGVQFRDVT TLMGNAQAFR RAVDELVYPY AGNRIDKVAG IEARGFILGG AIAHQLSAGF VPIRKKGKLP RDTVRIAYSL EYGVDEMEMH RDAIEKGERV VLVDDLIATG GTAEAAAKLL LQMGAEIVAA CFIIDLPDLG GRKKLEALGL PVRTLVAFEG D // ID APT_BRUME Reviewed; 181 AA. AC P63542; Q8YIG8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BMEI0476; OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=224914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16M / ATCC 23456 / NCTC 10094; RX PubMed=11756688; DOI=10.1073/pnas.221575398; RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., RA Haselkorn R., Kyrpides N.C., Overbeek R.; RT "The genome sequence of the facultative intracellular pathogen RT Brucella melitensis."; RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL51657.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE008917; AAL51657.1; ALT_INIT; Genomic_DNA. DR PIR; AF3311; AF3311. DR RefSeq; WP_002964645.1; NZ_GG703780.1. DR ProteinModelPortal; P63542; -. DR SMR; P63542; 8-181. DR STRING; 224914.BAWG_2452; -. DR PRIDE; P63542; -. DR EnsemblBacteria; AAL51657; AAL51657; BMEI0476. DR GeneID; 3788616; -. DR KEGG; bme:BMEI0476; -. DR PATRIC; 17851050; VBIBruMel92729_0535. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BMEL224914:GCJ0-497-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000419; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 181 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149364. SQ SEQUENCE 181 AA; 19614 MW; 128ABF9D88C2A953 CRC64; MESGFKVTLK DAIRTIPDYP KPGVQFRDVT TLMGNAQAFR RAVDELVYPY AGNRIDKVAG IEARGFILGG AIAHQLSAGF VPIRKKGKLP RDTVRIAYSL EYGVDEMEMH RDAIEKGERV VLVDDLIATG GTAEAAAKLL LQMGAEIVAA CFIIDLPDLG GRKKLEALGL PVRTLVAFEG D // ID APT_BRUO2 Reviewed; 181 AA. AC A5VRR9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BOV_1489; OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=444178; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512; RX PubMed=19436743; DOI=10.1371/journal.pone.0005519; RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M., RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T., RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S., RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.; RT "Genome degradation in Brucella ovis corresponds with narrowing of its RT host range and tissue tropism."; RL PLoS ONE 4:E5519-E5519(2009). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000708; ABQ60340.1; -; Genomic_DNA. DR RefSeq; WP_002964645.1; NC_009505.1. DR ProteinModelPortal; A5VRR9; -. DR SMR; A5VRR9; 8-181. DR PRIDE; A5VRR9; -. DR EnsemblBacteria; ABQ60340; ABQ60340; BOV_1489. DR GeneID; 3788616; -. DR KEGG; bov:BOV_1489; -. DR PATRIC; 17862986; VBIBruOvi136990_2888. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BOVI444178:GH2V-1488-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000006383; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 181 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000263. SQ SEQUENCE 181 AA; 19614 MW; 128ABF9D88C2A953 CRC64; MESGFKVTLK DAIRTIPDYP KPGVQFRDVT TLMGNAQAFR RAVDELVYPY AGNRIDKVAG IEARGFILGG AIAHQLSAGF VPIRKKGKLP RDTVRIAYSL EYGVDEMEMH RDAIEKGERV VLVDDLIATG GTAEAAAKLL LQMGAEIVAA CFIIDLPDLG GRKKLEALGL PVRTLVAFEG D // ID APT_BORA1 Reviewed; 182 AA. AC Q2KUE4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 09-DEC-2015, entry version 67. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=BAV3106; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=197N; RX PubMed=16885469; DOI=10.1128/JB.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., RA Squares S., Woodward J., Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella RT avium with those of B. bronchiseptica, B. pertussis, and B. RT parapertussis reveals extensive diversity in surface structures RT associated with host interaction."; RL J. Bacteriol. 188:6002-6015(2006). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM167904; CAJ50716.1; -; Genomic_DNA. DR RefSeq; WP_012418744.1; NC_010645.1. DR ProteinModelPortal; Q2KUE4; -. DR STRING; 360910.BAV3106; -. DR EnsemblBacteria; CAJ50716; CAJ50716; BAV3106. DR KEGG; bav:BAV3106; -. DR PATRIC; 21132524; VBIBorAvi43433_3140. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BAVI360910:GCKI-3180-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001977; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 182 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000259. SQ SEQUENCE 182 AA; 20131 MW; 224AA2F240F2F124 CRC64; MQTDYAEVVR RTIRSVPDWP VPGVTFRDIT PVLQDPRTFR ALVDLFVYRY MRQRLDLVAG VDARGFILGS VLAYELNLGF VPVRKKGKLP YRTVAEEYSL EYGNATVEIH TDAVRTGQRV LLVDDLIATG GTMVAAIKLL QRLGANVVEA AAIIDLPYIG GSQHIAETGT PLYTVCQFSA TD // ID APT_BIFAA Reviewed; 193 AA. AC A1A1K5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BAD_0807; OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC OS 11814 / E194a). OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=367928; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a; RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., RA Hirai S., Tanaka K., Watanabe K.; RT "Bifidobacterium adolescentis complete genome sequence."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009256; BAF39588.1; -; Genomic_DNA. DR RefSeq; WP_011743182.1; NC_008618.1. DR ProteinModelPortal; A1A1K5; -. DR STRING; 367928.BAD_0807; -. DR EnsemblBacteria; BAF39588; BAF39588; BAD_0807. DR GeneID; 4557211; -. DR KEGG; bad:BAD_0807; -. DR PATRIC; 21101003; VBIBifAdo27973_0874. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; FYKLDGK; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BADO367928:GHPT-845-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000008702; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 193 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000258. SQ SEQUENCE 193 AA; 20237 MW; A615646DA87CAA2F CRC64; MAASDITVSG LNKVGAEDAA YLVSKIRTIP GFPKEGILFR DFMPVLADAR AFGILMGALE AALPVDVDDF DMVVGLEARG FLFGPALAAR LGKGFIAVRK AGKLPPETMS QSYDLEYGQA SMEIETNVVH EGVRVLIVDD LIATGGTANA ARSLIEKCGG VVAGFSFVME LTGIDGMKSL GDYPTSSLVC MPA // ID APT_BACP2 Reviewed; 170 AA. AC A8FFQ0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 16-MAR-2016, entry version 59. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BPUM_2402; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=315750; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., RA Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C., RA Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., RA Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., RA Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., RA Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., RA Venkateswaran K., Highlander S.K., Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000813; ABV63067.1; -; Genomic_DNA. DR RefSeq; WP_003216770.1; NC_009848.2. DR ProteinModelPortal; A8FFQ0; -. DR STRING; 315750.BPUM_2402; -. DR EnsemblBacteria; ABV63067; ABV63067; BPUM_2402. DR KEGG; bpu:BPUM_2402; -. DR PATRIC; 18968724; VBIBacPum16546_2457. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BPUM315750:GH6N-2459-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000057029. SQ SEQUENCE 170 AA; 18874 MW; 7FE72F0CAD41A6E4 CRC64; MDLKQYVTVV PDYPKEGVQF KDITTLMDKG EVYRYATDQI VEYAKERDID LIVGPEARGF IIGCPVAYAL GVGFAPVRKE GKLPREVVKV EYGLEYGKDV LTIHKDAIRP GQRVLITDDL LATGGTIEAS IKLVEELGGV VAGIAFLIEL TYLDGRKKLD GYDILTLMQY // ID APT_BDEBA Reviewed; 165 AA. AC Q6MPK7; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=Bd0845; OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 OS / HD100). OC Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales; OC Bdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=264462; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15356 / DSM 50701 / NCIB 9529 / HD100; RX PubMed=14752164; DOI=10.1126/science.1093027; RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., RA Sockett R.E., Schuster S.C.; RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a RT genomic perspective."; RL Science 303:689-692(2004). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX842648; CAE78790.1; -; Genomic_DNA. DR RefSeq; WP_011163392.1; NC_005363.1. DR ProteinModelPortal; Q6MPK7; -. DR STRING; 264462.Bd0845; -. DR EnsemblBacteria; CAE78790; CAE78790; Bd0845. DR KEGG; bba:Bd0845; -. DR PATRIC; 21076364; VBIBdeBac73187_0769. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; FYKLDGK; -. DR OrthoDB; EOG6T4S55; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000008080; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 165 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149356. SQ SEQUENCE 165 AA; 18006 MW; 5A648C5DD6C085FF CRC64; MDLKSLIRDV PDFPKPGIIF RDMSPLLQNA EALSFVSHNL LKHVDLTHVD YFAGIESRGF ILAAHMAATH KKGFLPIRKA GKLPPPTRKV SYALEYGTAE IELPPGRGNV VIVDDVLATG GTLQAAIDLC LLAGYSVESV AVLVNLTFLN KMTYNDQKVA SLVQY // ID APT_BORPA Reviewed; 191 AA. AC Q7W3L2; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=BPP4020; OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=257311; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX640435; CAE39303.1; -; Genomic_DNA. DR ProteinModelPortal; Q7W3L2; -. DR EnsemblBacteria; CAE39303; CAE39303; BPP4020. DR KEGG; bpa:BPP4020; -. DR PATRIC; 21152124; VBIBorPar43418_4220. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BPAR257311:BPP4020-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001421; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 191 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149361. SQ SEQUENCE 191 AA; 21136 MW; F137433B3A4A1C9E CRC64; MLLFPGTFTM QTDYAELVRR TIRSVPDWPT PGVTFRDITP VLQDPRTFRV LIDLFVYRYM RQRLDLVAGV DARGFIVGAV LAHELNLGFV PVRKKGKLPY RTVAEEYSLE YGNAAVEMHT DSVRTGQRVL LVDDLIATGG TMLAAIKLLQ RLGANVVEAA AIIDLPYLGG SAQITATGTP LYTVCQYQEG D // ID APT_BURP0 Reviewed; 187 AA. AC A3NRB5; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 11-NOV-2015, entry version 54. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BURPS1106A_0604; OS Burkholderia pseudomallei (strain 1106a). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=357348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1106a; RA DeShazer D., Woods D.E., Nierman W.C.; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC -!- SEQUENCE CAUTION: CC Sequence=ABN92536.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000572; ABN92536.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_004534111.1; NC_009076.1. DR ProteinModelPortal; A3NRB5; -. DR EnsemblBacteria; ABN92536; ABN92536; BURPS1106A_0604. DR KEGG; bpl:BURPS1106A_0604; -. DR PATRIC; 19219784; VBIBurPse14980_0577. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BPSE357348:GHVF-603-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000006738; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 187 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321347. SQ SEQUENCE 187 AA; 20208 MW; F5E98CD2BBB43659 CRC64; MMSTSDAPLD PVEFIHSRIR TVPDWPQPGV MFRDITPLLQ SAKALRVLVD LFVERYVDAK LDYIAGLDAR GFIIAPIVAY ELSVGFVPIR KVGKLPYATQ RESYALEYGT ATVEIHEDAC KPGDRVVIVD DLIATGGTMM AGKNLLERLG AVVVEGAAIV DLPDLGGSAL LRGAGLPLYT VTEFPGH // ID APT_BURP8 Reviewed; 188 AA. AC B2JCQ7; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 11-NOV-2015, entry version 50. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Bphy_0333; OS Burkholderia phymatum (strain DSM 17167 / STM815). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=391038; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17167 / STM815; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D., RA Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Bacher J., Blanchard J., Cohan F., RA James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P., RA Riley M., Souza V., Wertz J., Young P.; RT "Complete sequence of chromosome 1 of Burkholderia phymatum STM815."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001043; ACC69526.1; -; Genomic_DNA. DR RefSeq; WP_012399752.1; NC_010622.1. DR ProteinModelPortal; B2JCQ7; -. DR STRING; 391038.Bphy_0333; -. DR EnsemblBacteria; ACC69526; ACC69526; Bphy_0333. DR KEGG; bph:Bphy_0333; -. DR PATRIC; 19186781; VBIBurPhy25146_0347. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BPHY391038:GI4Z-338-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001192; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 188 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088959. SQ SEQUENCE 188 AA; 20519 MW; 71D2A2807CC99706 CRC64; MSHAPANRPF DPAEYINSEI RTVPDWPQAG VQFRDITPLL QKPKSLRVLI DLFVQRYIDQ KLDYVAGLDA RGFIIGPILA YELNLGFIPI RKIGKLPFRT VSESYELEYG SATVEIHEDA CKPGDRVVIV DDLIATGGTM MAGKKLLERL GATVIEGAAI VDLPDLGGSK LLRGAGLPLF TVTSFGGH // ID APT_BURL3 Reviewed; 188 AA. AC Q39CV8; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Bcep18194_A6114; OS Burkholderia lata (strain ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 OS / 383). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=482957; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 / 383; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia sp. 383."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000151; ABB09708.1; -; Genomic_DNA. DR RefSeq; WP_011353218.1; NZ_LDWP01000060.1. DR ProteinModelPortal; Q39CV8; -. DR EnsemblBacteria; ABB09708; ABB09708; Bcep18194_A6114. DR KEGG; bur:Bcep18194_A6114; -. DR PATRIC; 19289761; VBIBurSp120713_4256. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BSP269483:GHLS-3002-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002705; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 188 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321349. SQ SEQUENCE 188 AA; 20392 MW; 4634C22FC837077F CRC64; MPHSSSGAPL DPVAFIHSQI RTVPDWPQPG VMFRDITTLL QSPKALRILV DLFVERYVDA KLDYVAGLDA RGFIIAPIVA YELSVGFVPI RKVGKLPYKT RSESYDLEYG SATVEIHEDA CRPGDRVIIM DDLIATGGTM MAGRNLLQRL GAEVVEGAAI IDLPDLGGSA LLRNAGLPVY TVTEFAGH // ID APT_BUTFI Reviewed; 180 AA. AC O31060; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 22-JUL-2015, entry version 75. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; Synonyms=aptA; OS Butyrivibrio fibrisolvens. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=831; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=OR77; RA Kalmokoff M.L., Allard S., Austin J.W., Whitford M., Hefford M.A., RA Teather R.M.; RT "Isolation, sequencing, and transcriptional analysis of the flagellins RT from the rumen anaerobe Butyrivibrio fibrisolvens OR77: evidence RT supporting post-translational modification of these flagellins."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF026811; AAB82611.1; -; Genomic_DNA. DR ProteinModelPortal; O31060; -. DR UniPathway; UPA00588; UER00646. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase. FT CHAIN 1 180 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149367. SQ SEQUENCE 180 AA; 19663 MW; 9A1FB4807BB2AB49 CRC64; MKKVEDYIRT IPDFPEPGIM FRDVTSILQD AEGFKLAIDE MIKLLDGVDC DVIAGAESRG FIFGAPLAYA LGKPSVLVRK KGKLPCETIE KTYDLEYGTA TIEMHKDAIK PGQKVVVVDD LIATGGTIEA ACQLIEELGG EVSKIVFLME LAGLNGREKL KYDVASVCYL RGKIITDFLG // ID APT_BURPS Reviewed; 187 AA. AC Q63XK0; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=BPSL0540; OS Burkholderia pseudomallei (strain K96243). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=272560; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., RA Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A., RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, RT Burkholderia pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571965; CAH34529.1; -; Genomic_DNA. DR RefSeq; WP_004534111.1; NZ_CP009538.1. DR RefSeq; YP_107165.1; NC_006350.1. DR ProteinModelPortal; Q63XK0; -. DR STRING; 272560.BPSL0540; -. DR EnsemblBacteria; CAH34529; CAH34529; BPSL0540. DR GeneID; 3094203; -. DR KEGG; bps:BPSL0540; -. DR PATRIC; 19260747; VBIBurPse99623_0604. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; BPSE272560:GJNI-549-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000605; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 187 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149366. SQ SEQUENCE 187 AA; 20208 MW; F5E98CD2BBB43659 CRC64; MMSTSDAPLD PVEFIHSRIR TVPDWPQPGV MFRDITPLLQ SAKALRVLVD LFVERYVDAK LDYIAGLDAR GFIIAPIVAY ELSVGFVPIR KVGKLPYATQ RESYALEYGT ATVEIHEDAC KPGDRVVIVD DLIATGGTMM AGKNLLERLG AVVVEGAAIV DLPDLGGSAL LRGAGLPLYT VTEFPGH // ID APT_CHLTE Reviewed; 177 AA. AC Q8KFM9; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=CT0293; OS Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / OS TLS). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=194439; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS; RX PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., RA Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., RA Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., RA Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., RA Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., RA Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., RA Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a RT photosynthetic, anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE006470; AAM71539.1; -; Genomic_DNA. DR RefSeq; NP_661197.1; NC_002932.3. DR RefSeq; WP_010931985.1; NC_002932.3. DR ProteinModelPortal; Q8KFM9; -. DR STRING; 194439.CT0293; -. DR EnsemblBacteria; AAM71539; AAM71539; CT0293. DR GeneID; 1007952; -. DR KEGG; cte:CT0293; -. DR PATRIC; 21398701; VBIChlTep116050_0284. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CTEP194439:GHN0-309-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001007; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 177 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149371. SQ SEQUENCE 177 AA; 19319 MW; A060D2DD9C242B41 CRC64; MPIKSRIRTV PDYPKKGIMF RDITTLIKDP VGFRLVIDNM TQHYLSNGVD FDAIVGIESR GFILGGALAY TLGKGFVPVR KPGKLPADVV QLEYELEYGT DKIEMHTDAL VQGQRVLLVD DLLATGGTAL AAAGLVEKLG GVVASMAFIV NLPDIGGEKK IREKGYNIYF LTEFEGD // ID APT_CLOBK Reviewed; 172 AA. AC B1IME3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 11-NOV-2015, entry version 50. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CLD_1480; OS Clostridium botulinum (strain Okra / Type B1). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=498213; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Okra / Type B1; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1- RT A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000939; ACA46221.1; -; Genomic_DNA. DR RefSeq; WP_003357763.1; NC_010516.1. DR ProteinModelPortal; B1IME3; -. DR EnsemblBacteria; ACA46221; ACA46221; CLD_1480. DR KEGG; cbb:CLD_1480; -. DR PATRIC; 19406552; VBICloBot127283_3177. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CBOT498213:GCNI-3127-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000008541; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000334713. SQ SEQUENCE 172 AA; 19130 MW; ABC189082347D3D7 CRC64; MNLKEHIRVI ENFPKEGISF KDVTTILQDG KVLNYTIDKL AENLKDKKID KIVGPEARGF LFGTPLAYKL GVGFVPVRKK GKLPYETISC KYDLEYGQDE LQIHKDSIKK GDKVAIVDDL LATGGTIASV VKLVEELGGE VVNVSFVIEL TDLKGKDKLE GYDINSLVQY NI // ID APT_CHLPD Reviewed; 177 AA. AC A1BDK4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Cpha266_0423; OS Chlorobium phaeobacteroides (strain DSM 266). OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; OC Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290317; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 266; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., RA Overmann J., Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobium phaeobacteroides DSM 266."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000492; ABL64481.1; -; Genomic_DNA. DR RefSeq; WP_011744314.1; NC_008639.1. DR ProteinModelPortal; A1BDK4; -. DR STRING; 290317.Cpha266_0423; -. DR EnsemblBacteria; ABL64481; ABL64481; Cpha266_0423. DR KEGG; cph:Cpha266_0423; -. DR PATRIC; 21388577; VBIChlPha122104_0475. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; VHALCAF; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CPHA290317:GHX4-433-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000008701; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 177 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000000273. SQ SEQUENCE 177 AA; 19114 MW; 58EEDD39A5B61E3E CRC64; MTIKSRIRSI PDYPKKGIMF RDITTLIKDP VGFRLVIDNL TQHYLQNGVD FDVIVGIEAR GFIIGGALSY ALGKGFVPVR KPGKLPADVA SQKYELEYGS DTIEIHIDAL EEGSRVLLVD DLLATGGTAL AAAALVEKVG GVVAEMAFIV NLPDVGGEQR ILDKGYSIFS LTDFEGD // ID APT_CUPPJ Reviewed; 190 AA. AC Q476D8; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 16-MAR-2016, entry version 73. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Reut_A0363; OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia OS eutropha (strain JMP 134)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=264198; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JMP134 / LMG 1197; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., RA Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC -!- SEQUENCE CAUTION: CC Sequence=AAZ59745.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000090; AAZ59745.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_041679800.1; NC_007347.1. DR ProteinModelPortal; Q476D8; -. DR STRING; 264198.Reut_A0363; -. DR EnsemblBacteria; AAZ59745; AAZ59745; Reut_A0363. DR KEGG; reu:Reut_A0363; -. DR PATRIC; 20226175; VBIRalEut24049_0964. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CPIN264198:GIW3-365-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002697; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 190 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321389. SQ SEQUENCE 190 AA; 20745 MW; 2A1729DD9596A575 CRC64; MADSLIQSPD LGDVTGYLRD RIRTVPDWPM PGVQFRDITP LLQNPKTLRV LIDVFVHRYM DAQLDLVAGI DARGFILGAI VAYELNLGFV PIRKKGKLPF QTVAEEYELE YGSATVEIHA DACKPGDRVL LIDDLIATGG TMMAGRKLLE RLGATVVEGA AIVDLPELGG SKLLQNAGLP LFTVCRFDGH // ID APT_CLOB8 Reviewed; 172 AA. AC A6LTN5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Cbei_1539; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Tapia R., Brainard J., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Bennet G., Cann I., Chen J.-S., Contreras A.L., RA Jones D., Kashket E., Mitchell W., Stoddard S., Schwarz W., RA Qureshi N., Young M., Shi Z., Ezeji T., White B., Blaschek H., RA Richardson P.; RT "Complete sequence of Clostridium beijerinckii NCIMB 8052."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000721; ABR33715.1; -; Genomic_DNA. DR RefSeq; WP_011968867.1; NC_009617.1. DR ProteinModelPortal; A6LTN5; -. DR STRING; 290402.Cbei_1539; -. DR EnsemblBacteria; ABR33715; ABR33715; Cbei_1539. DR KEGG; cbe:Cbei_1539; -. DR PATRIC; 19347090; VBICloBei69853_1587. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CBEI290402:GHL5-1615-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000565; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000073788. SQ SEQUENCE 172 AA; 18759 MW; C3C4098F5E70DC16 CRC64; MDLQEKIRVI ENFPKEGISF KDITTLIADG EALRETINRI VKHLEDKKID LIVGPEARGF IFGVPVAYAL GVGFIPVRKP GKLPGETISV NYGLEYGEDQ LQLHKDAIKP GQRVAVVDDL LATGGTVEGV AKLIEQAGGI VASLDFVIEL TELKGKDKLE GYDVLSLVKY DI // ID APT_CLOB1 Reviewed; 172 AA. AC A7FY09; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CLB_3089; OS Clostridium botulinum (strain ATCC 19397 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=441770; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19397 / Type A; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1- RT A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000726; ABS33533.1; -; Genomic_DNA. DR RefSeq; WP_003357763.1; NC_009697.1. DR ProteinModelPortal; A7FY09; -. DR EnsemblBacteria; ABS33533; ABS33533; CLB_3089. DR KEGG; cba:CLB_3089; -. DR PATRIC; 19360720; VBICloBot110701_2992. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CBOT441770:GH1E-3055-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000329339. SQ SEQUENCE 172 AA; 19130 MW; ABC189082347D3D7 CRC64; MNLKEHIRVI ENFPKEGISF KDVTTILQDG KVLNYTIDKL AENLKDKKID KIVGPEARGF LFGTPLAYKL GVGFVPVRKK GKLPYETISC KYDLEYGQDE LQIHKDSIKK GDKVAIVDDL LATGGTIASV VKLVEELGGE VVNVSFVIEL TDLKGKDKLE GYDINSLVQY NI // ID APT_DESMR Reviewed; 171 AA. AC C4XU70; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 16-MAR-2016, entry version 45. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=DMR_26010; OS Desulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=573370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700980 / DSM 13731 / RS-1; RX PubMed=19675025; DOI=10.1101/gr.088906.108; RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., RA Aoki N., Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., RA Takeyama H., Matsunaga T.; RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 RT revealed common gene clusters in magnetotactic bacteria."; RL Genome Res. 19:1801-1808(2009). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP010904; BAH76092.1; -; Genomic_DNA. DR RefSeq; WP_015861269.1; NC_012796.1. DR ProteinModelPortal; C4XU70; -. DR STRING; 573370.DMR_26010; -. DR EnsemblBacteria; BAH76092; BAH76092; DMR_26010. DR KEGG; dma:DMR_26010; -. DR PATRIC; 21751479; VBIDesMag26496_2503. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; DMAG573370:GHJL-2630-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000009071; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 171 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000201660. SQ SEQUENCE 171 AA; 18682 MW; 069B615775F1EC9F CRC64; MDLRQLIRDI PDYPKEGILF FDITPLLGDP DGFRRAIDLL AERFADSGAT KIVAAEARGF IFGAALAYKM GLGFVPVRKP GKLPYKTVSV SYDLEYGSDT LCMHEDALLR DEKVLVIDDL LATGGTLSGV IDLVEHFGAD IVGIGVVIEL EFLNGKEQLR SYGCESILQI A // ID APT_CLOP1 Reviewed; 172 AA. AC Q0TP22; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CPF_2194; OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / OS NCIMB 6125 / NCTC 8237 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S RC 107 / Type A; RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000246; ABG83902.1; -; Genomic_DNA. DR RefSeq; WP_003451591.1; NC_008261.1. DR ProteinModelPortal; Q0TP22; -. DR STRING; 195103.CPF_2194; -. DR EnsemblBacteria; ABG83902; ABG83902; CPF_2194. DR GeneID; 990253; -. DR KEGG; cpf:CPF_2194; -. DR PATRIC; 19486640; VBICloPer106549_2134. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CPER195103:GHAW-2208-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001823; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000329342. SQ SEQUENCE 172 AA; 18602 MW; 45938D903A9E3C7E CRC64; MSLKDKIRVI EDFPKKGISF KDITTLIADG EGLRDSVDQM AEFFKDKNID VVVGPEARGF IFGVPVAYAL GVGFIPVRKP GKLPGDTVRV EYDLEYGKDA LEIHKDAIKP GMRVAIVDDL LATGGTIAAV AKLVEQAGGE VAGLAFTIEL TELKGRDKLK GYEVTSLVDY DV // ID APT_CLOK5 Reviewed; 172 AA. AC A5N1Z4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CKL_3132; OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=431943; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680; RX PubMed=18218779; DOI=10.1073/pnas.0711093105; RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H., RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., RA Hagemeier C., Thauer R.K., Gottschalk G.; RT "The genome of Clostridium kluyveri, a strict anaerobe with unique RT metabolic features."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000673; EDK35140.1; -; Genomic_DNA. DR RefSeq; WP_012103475.1; NC_009706.1. DR ProteinModelPortal; A5N1Z4; -. DR STRING; 431943.CKL_3132; -. DR EnsemblBacteria; EDK35140; EDK35140; CKL_3132. DR KEGG; ckl:CKL_3132; -. DR PATRIC; 19467814; VBICloKlu111549_3237. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; GTDFFQM; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CKLU431943:GJF1-3125-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000002411; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000073789. SQ SEQUENCE 172 AA; 18928 MW; E94F38197E4A96DF CRC64; MNLQDNIRIV EGFPKKGISF KDITTLIRDK DAFKYAVDKI AGYLKDKNID VVVGPEARGF LFGAPIAYTL GAGFVPVRKQ GKLPYDTLSI KYDLEYGSDV LQIHKDAINK GDRVALVDDL LATGGTTSSV VKLIEQAGGE IVTIDFVIEL TDLKGREKLK GYDVLSLIKY DI // ID APT_COREF Reviewed; 192 AA. AC Q8FPL0; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2003, sequence version 2. DT 09-DEC-2015, entry version 74. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=CE1768; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM OS 11189 / NBRC 100395). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., RA Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., RA Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC18578.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000035; BAC18578.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_006767765.1; NZ_GG700683.1. DR ProteinModelPortal; Q8FPL0; -. DR STRING; 196164.HMPREF0290_1799; -. DR EnsemblBacteria; BAC18578; BAC18578; BAC18578. DR KEGG; cef:CE1768; -. DR PATRIC; 21489673; VBICorEff9312_1757. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CEFF196164:GJW8-1797-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001409; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 192 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149377. SQ SEQUENCE 192 AA; 19991 MW; 58946B4EB2251A27 CRC64; MDSGRDSGND SGSVNMARAR VALTEHTRYV HDFPAEGVLF EDLTPVLANA EAFAAVVDAQ AEAAEELGAE IIGGLDARGF LLGSAVAYKL GLGVIAIRKK GKLPPPVVTQ DYDLEYGSAA LELPAEGLDL EGRRVVLIDD VLATGGTLAA ARKLIETCGG NVTGYVLAIE VGGLGGRERL GDIPVHVIRD PQ // ID APT_CLOTE Reviewed; 172 AA. AC Q892A7; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CTC_02200; OS Clostridium tetani (strain Massachusetts / E88). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=212717; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Massachusetts / E88; RX PubMed=12552129; DOI=10.1073/pnas.0335853100; RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., RA Gottschalk G.; RT "The genome sequence of Clostridium tetani, the causative agent of RT tetanus disease."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE015927; AAO36688.1; -; Genomic_DNA. DR RefSeq; WP_011100349.1; NC_004557.1. DR ProteinModelPortal; Q892A7; -. DR STRING; 212717.CTC02200; -. DR EnsemblBacteria; AAO36688; AAO36688; CTC_02200. DR GeneID; 24254009; -. DR KEGG; ctc:CTC02200; -. DR PATRIC; 19512507; VBICloTet101274_2299. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CTET212717:GJAM-2020-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001412; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149375. SQ SEQUENCE 172 AA; 18962 MW; 704C8B4F9A77885E CRC64; MDLKDKIRVI QGFPKEGISF KDVTTILQEK EAFKYTIDTL VEELKDKNVD VVVGPEARGF LFGAPLAYAL GAGFVPVRKK GKLPSTTISS KYELEYGSDE LEMHKDSIKP GQRVVIADDL LATGGTICSV IEMIESLGGE IVSINFLIEL TDLKGREKLG KYDISSLVQY DI // ID APT_DICNV Reviewed; 174 AA. AC A5EVW7; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=DNO_0414; OS Dichelobacter nodosus (strain VCS1703A). OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales; OC Cardiobacteriaceae; Dichelobacter. OX NCBI_TaxID=246195; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VCS1703A; RX PubMed=17468768; DOI=10.1038/nbt1302; RA Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., RA Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., RA Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., RA Holley T., Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., RA Adler B., Songer J.G., Rood J.I., Paulsen I.T.; RT "Genome sequence and identification of candidate vaccine antigens from RT the animal pathogen Dichelobacter nodosus."; RL Nat. Biotechnol. 25:569-575(2007). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000513; ABQ13670.1; -; Genomic_DNA. DR ProteinModelPortal; A5EVW7; -. DR STRING; 246195.DNO_0414; -. DR EnsemblBacteria; ABQ13670; ABQ13670; DNO_0414. DR KEGG; dno:DNO_0414; -. DR PATRIC; 21785134; VBIDicNod48475_0412. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; DNOD246195:GHHS-414-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000248; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 174 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321360. SQ SEQUENCE 174 AA; 19122 MW; A22841AFE61E3815 CRC64; MNMDWKNLII NIPDYPKAGI NFKDITPLLA NGAGFKAAIE EMAMICERQN AIPDVLACPE ARGFIFAAAL AHRLGIGFIP LRKPHKLPRE VAHINYGLEY GEDCLEVHKQ DIKKGMRIMM VDDVLATGGT MHACMNLLQS LGAEIIGAMF LLELTALKGR EKLGTAAVYS LIQD // ID APT_CORJK Reviewed; 207 AA. AC Q4JVE4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=jk1049; OS Corynebacterium jeikeium (strain K411). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=306537; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K411; RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005; RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., RA Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., RA Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., RA Puehler A.; RT "Complete genome sequence and analysis of the multiresistant RT nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring RT bacterium of the human skin flora."; RL J. Bacteriol. 187:4671-4682(2005). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR931997; CAI37213.1; -; Genomic_DNA. DR ProteinModelPortal; Q4JVE4; -. DR STRING; 306537.jk1049; -. DR EnsemblBacteria; CAI37213; CAI37213; jk1049. DR KEGG; cjk:jk1049; -. DR PATRIC; 21513010; VBICorJei31838_1061. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CJEI306537:GJ8V-1084-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000545; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 207 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000321358. SQ SEQUENCE 207 AA; 22166 MW; 32AE14BC92640198 CRC64; MRPAKPPQSK ERKRSKSLTS ADHDNSPQRA ETAASALRQR IRVVPDFPSR GIVFEDLTPV LADPHSFKLL VQDLANHCRN FDIDLIGGLD ARGFLLGSAV AYELGVGILA VRKGGKLPPP VHHVDYSLEY GTASLEIPAD NAIPLQGKNV FLIDDVLATG GTLSASRELL ENAGANVCGL GVVLEVSALD GRDRLKDLPL YVVDQAG // ID APT_DEBHA Reviewed; 186 AA. AC Q6BZF9; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Adenine phosphoribosyltransferase; DE Short=APRT; DE EC=2.4.2.7; GN Name=APT1; OrderedLocusNames=DEHA2A01650g; OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC OS 0083 / IGC 2968) (Yeast) (Torulaspora hansenii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces. OX NCBI_TaxID=284592; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR382133; CAG84362.1; -; Genomic_DNA. DR RefSeq; XP_456410.1; XM_456410.1. DR ProteinModelPortal; Q6BZF9; -. DR SMR; Q6BZF9; 6-177. DR EnsemblFungi; CAG84362; CAG84362; DEHA2A01650g. DR GeneID; 2899963; -. DR KEGG; dha:DEHA2A01650g; -. DR HOGENOM; HOG000036776; -. DR InParanoid; Q6BZF9; -. DR KO; K00759; -. DR OMA; GTDFFQM; -. DR OrthoDB; EOG7WT4CC; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000599; Chromosome A. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006168; P:adenine salvage; IEA:InterPro. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Magnesium; KW Metal-binding; Nucleus; Purine salvage; Reference proteome; KW Transferase. FT CHAIN 1 186 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000227900. FT NP_BIND 132 136 AMP. {ECO:0000250}. SQ SEQUENCE 186 AA; 20387 MW; 71430CEC86CA0FD7 CRC64; MSQVEISELA KEIRASLKQF PNFPSEGILF EDFLPVFTKP DLFQKLVRAF QLHVGEQKVD YVVGLESRGF LFGPTLALAL GAGFVPVRKA GKLPGPVFTA EFQKEYGSDK FQIQKDVIEE GAKVLIVDDI LATGGSASSA GELVKQTGGD IVEYLFVMEL DFLNGRDKLD KPAFTLLSGQ AEKLQN // ID APT_CORGL Reviewed; 185 AA. AC O87330; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Cgl1654, cg1862; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / OS LMG 3730 / NCIMB 10025). OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX PubMed=9695918; RA Wehmeier L., Schaefer A., Burkovski A., Kraemer R., Mechold U., RA Malke H., Puehler A., Kalinowski J.; RT "The role of the Corynebacterium glutamicum rel gene in (p)ppGpp RT metabolism."; RL Microbiology 144:1853-1862(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., RA Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence RT and its impact on the production of L-aspartate-derived amino acids RT and vitamins."; RL J. Biotechnol. 104:5-25(2003). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF038651; AAC35493.1; -; Genomic_DNA. DR EMBL; BA000036; BAB99047.1; -; Genomic_DNA. DR EMBL; BX927153; CAF20037.1; -; Genomic_DNA. DR RefSeq; NP_600867.1; NC_003450.3. DR RefSeq; WP_011014514.1; NC_006958.1. DR ProteinModelPortal; O87330; -. DR STRING; 196627.cg1862; -. DR EnsemblBacteria; BAB99047; BAB99047; BAB99047. DR EnsemblBacteria; CAF20037; CAF20037; cg1862. DR GeneID; 1019622; -. DR KEGG; cgb:cg1862; -. DR KEGG; cgl:NCgl1591; -. DR PATRIC; 21495344; VBICorGlu203724_1615. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000582; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 185 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000149378. SQ SEQUENCE 185 AA; 19563 MW; FDBAC03A3FF18182 CRC64; MSEQALSTFD RAREALDKKT RYVQDFPEKG VLFEDLTPVL GDAESFVAVV DAMAEAAEKL NAEIIGGLDA RGFLLGSAVA YKLGLGVLAI RKKGKLPPPV VTQEYELEYG TAALELPSEG IDIAGKNIVL IDDVLATGGT LGAARKLIES CDGHVSGYVL AIEVPGLGGR DNLGDRPVIV VRDPQ // ID APT_ECOHS Reviewed; 183 AA. AC A7ZXC7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=EcHS_A0546; OS Escherichia coli O9:H4 (strain HS). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331112; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HS; RX PubMed=18676672; DOI=10.1128/JB.00619-08; RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., RA Henderson I.R., Sperandio V., Ravel J.; RT "The pangenome structure of Escherichia coli: comparative genomic RT analysis of E. coli commensal and pathogenic isolates."; RL J. Bacteriol. 190:6881-6893(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000802; ABV04931.1; -; Genomic_DNA. DR RefSeq; WP_000127356.1; NC_009800.1. DR ProteinModelPortal; A7ZXC7; -. DR SMR; A7ZXC7; 2-183. DR PRIDE; A7ZXC7; -. DR EnsemblBacteria; ABV04931; ABV04931; EcHS_A0546. DR KEGG; ecx:EcHS_A0546; -. DR PATRIC; 18311082; VBIEscCol77814_0535. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; ECOL331112:GHHI-544-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase. FT CHAIN 1 183 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000057031. SQ SEQUENCE 183 AA; 19859 MW; AB45F0B5A219480D CRC64; MTATAQQLEY LKNSIKSIQD YPKPGILFRD VTSLLEDPKA YALSIDLLVE RYKNAGITKV VGTEARGFLF GAPVALGLGV GFVPVRKPGK LPRETISETY DLEYGTDQLE IHVDAIKPGD KVLVVDDLLA TGGTIEATVK LIRRLGGEVA DAAFIINLFD LGGEQRLEKQ GITSYSLVPF PGH // ID APT_DESHD Reviewed; 170 AA. AC B8FQU0; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 11-NOV-2015, entry version 46. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=Dhaf_3610; OS Desulfitobacterium hafniense (strain DCB-2 / DSM 10664). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; OC Desulfitobacterium. OX NCBI_TaxID=272564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DCB-2 / DSM 10664; RX PubMed=22316246; DOI=10.1186/1471-2180-12-21; RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., RA Marsh T.L., Tiedje J.M.; RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram- RT positive anaerobe capable of dehalogenation and metal reduction."; RL BMC Microbiol. 12:21-21(2012). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001336; ACL21627.1; -; Genomic_DNA. DR RefSeq; WP_015944687.1; NC_011830.1. DR ProteinModelPortal; B8FQU0; -. DR EnsemblBacteria; ACL21627; ACL21627; Dhaf_3610. DR KEGG; dhd:Dhaf_3610; -. DR PATRIC; 21665197; VBIDesHaf15223_3757. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; DHAF272564:GCV8-3684-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000007726; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 170 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000116238. SQ SEQUENCE 170 AA; 18495 MW; 2BB047EE47BA0D46 CRC64; MDFDKYIRVI DDFPKPGISF KDITTLLKDG EAYRAAVDAI VERVRESQPD LIVGPEARGF LLGAPVAYAL GIGFVPVRKP GKLPGKTVSE TYELEYGSDT LEVHADAIQP GQRIAIVDDL LATGGTTSAT ARLIEKTGAQ VAGMSFLIEL GFLEGRKRLE GYEVFSLIKY // ID APT_ECO5E Reviewed; 183 AA. AC B5Z3X9; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=ECH74115_0559; OS Escherichia coli O157:H7 (strain EC4115 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EC4115 / EHEC; RX PubMed=22135463; DOI=10.1073/pnas.1107176108; RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.; RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001164; ACI37693.1; -; Genomic_DNA. DR RefSeq; WP_001301904.1; NC_011353.1. DR ProteinModelPortal; B5Z3X9; -. DR SMR; B5Z3X9; 2-183. DR EnsemblBacteria; ACI37693; ACI37693; ECH74115_0559. DR KEGG; ecf:ECH74115_0559; -. DR PATRIC; 18361941; VBIEscCol74651_0676. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; ECOL444450:GHOB-555-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase. FT CHAIN 1 183 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088968. SQ SEQUENCE 183 AA; 19872 MW; AB45F0A04216A817 CRC64; MTATAQQLEY LKNSIKSIQD YPKPGILFRD VTSLLEDPKA YALSIDLLVE RYKNAGINKV VGTEARGFLF GAPVALGLGV GFVPVRKPGK LPRETISETY DLEYGTDQLE IHVDAIKPGD KVLVVDDLLA TGGTIEATVK LIRRLGGEVA DAAFIINLFD LGGEQRLEKQ GITSYSLVPF PGH // ID APT_CYAA5 Reviewed; 172 AA. AC B1WQD7; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 11-NOV-2015, entry version 51. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=cce_2298; OS Cyanothece sp. (strain ATCC 51142). OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales; OC Cyanothece. OX NCBI_TaxID=43989; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51142; RX PubMed=18812508; DOI=10.1073/pnas.0805418105; RA Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C., RA Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., RA Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.; RT "The genome of Cyanothece 51142, a unicellular diazotrophic RT cyanobacterium important in the marine nitrogen cycle."; RL Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000806; ACB51648.1; -; Genomic_DNA. DR RefSeq; WP_009545002.1; NC_010546.1. DR ProteinModelPortal; B1WQD7; -. DR STRING; 43989.cce_2298; -. DR EnsemblBacteria; ACB51648; ACB51648; cce_2298. DR KEGG; cyt:cce_2298; -. DR PATRIC; 21543029; VBICyaSp130209_2338. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CSP43989:GKC8-2332-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001203; Chromosome circular. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088967. SQ SEQUENCE 172 AA; 18880 MW; C20BDFFB98163B99 CRC64; MDLKGLIRDI PNFPKPGIVF RDITTLLSDA EGLRYTIDTL TEKCKAANLS PDYIVGMESR GFLFGVPLAY QLNAGFVPVR KPGKLPAAVH QVEYELEYGT DSLEIHQDAL NNHHNVLIVD DLMATGGTAK ATADLLEKIG CNVLGFAFII ELKALEGRKK LPNLPIISLV DY // ID APT_EDWI9 Reviewed; 183 AA. AC C5BCZ7; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 11-NOV-2015, entry version 43. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=NT01EI_1107; OS Edwardsiella ictaluri (strain 93-146). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Edwardsiella. OX NCBI_TaxID=634503; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=93-146; RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.; RT "Complete genome sequence of Edwardsiella ictaluri 93-146."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP001600; ACR68318.1; -; Genomic_DNA. DR RefSeq; WP_015870497.1; NC_012779.2. DR ProteinModelPortal; C5BCZ7; -. DR STRING; 634503.NT01EI_1107; -. DR EnsemblBacteria; ACR68318; ACR68318; NT01EI_1107. DR GeneID; 7960692; -. DR KEGG; eic:NT01EI_1107; -. DR PATRIC; 21835378; VBIEdwIct114273_1005. DR eggNOG; ENOG4109003; Bacteria. DR eggNOG; COG0503; LUCA. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; EICT634503:GCMY-1095-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000001485; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 183 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000201662. SQ SEQUENCE 183 AA; 19698 MW; 92283DBD71791865 CRC64; MTATAQQLEF LKQNIKTIPD YPKPGILFRD VTSLLEKPDA YALSIELLAA RYRAAGITKV VGTEARGFLF GAPVALALGV GFVPVRKPGK LPRATLAESY ALEYGTDTLE IHQDAIDAND RVLMVDDLLA TGGTIEATTR LIRRLGGVVH DAAFIIDLPA LGGEARLEAM NINCYSLVSF DGH // ID APT_ECOSE Reviewed; 183 AA. AC B6I0C1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=ECSE_0494; OS Escherichia coli (strain SE11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=409438; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SE11; RX PubMed=18931093; DOI=10.1093/dnares/dsn026; RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., RA Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.; RT "Complete genome sequence and comparative analysis of the wild-type RT commensal Escherichia coli strain SE11 isolated from a healthy RT adult."; RL DNA Res. 15:375-386(2008). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP009240; BAG76018.1; -; Genomic_DNA. DR RefSeq; WP_000127356.1; NC_011415.1. DR ProteinModelPortal; B6I0C1; -. DR SMR; B6I0C1; 2-183. DR PRIDE; B6I0C1; -. DR EnsemblBacteria; BAG76018; BAG76018; ECSE_0494. DR KEGG; ecy:ECSE_0494; -. DR PATRIC; 18419412; VBIEscCol83070_0623. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; ECOL409438:GHUU-502-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000008199; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 183 Adenine phosphoribosyltransferase. FT /FTId=PRO_1000088970. SQ SEQUENCE 183 AA; 19859 MW; AB45F0B5A219480D CRC64; MTATAQQLEY LKNSIKSIQD YPKPGILFRD VTSLLEDPKA YALSIDLLVE RYKNAGITKV VGTEARGFLF GAPVALGLGV GFVPVRKPGK LPRETISETY DLEYGTDQLE IHVDAIKPGD KVLVVDDLLA TGGTIEATVK LIRRLGGEVA DAAFIINLFD LGGEQRLEKQ GITSYSLVPF PGH // ID APT_CLOBM Reviewed; 172 AA. AC B1L0A2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 11-NOV-2015, entry version 49. DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004}; DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004}; DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004}; GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; GN OrderedLocusNames=CLK_2453; OS Clostridium botulinum (strain Loch Maree / Type A3). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=498214; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Loch Maree / Type A3; RX PubMed=18060065; DOI=10.1371/journal.pone.0001271; RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.; RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1- RT A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within RT plasmids."; RL PLoS ONE 2:E1271-E1271(2007). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of AMP, that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- CATALYTIC ACTIVITY: AMP + diphosphate = adenine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; CC AMP from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP- CC Rule:MF_00004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000962; ACA54636.1; -; Genomic_DNA. DR RefSeq; WP_012342715.1; NC_010520.1. DR ProteinModelPortal; B1L0A2; -. DR EnsemblBacteria; ACA54636; ACA54636; CLK_2453. DR KEGG; cbl:CLK_2453; -. DR PATRIC; 19391522; VBICloBot822_3371. DR HOGENOM; HOG000036776; -. DR KO; K00759; -. DR OMA; ATVEIHA; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; CBOT498214:GH05-3107-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000722; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1. DR InterPro; IPR005764; Ade_phspho_trans. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01090; apt; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Transferase. FT CHAIN 1 172 Adenine phosphoribosyltransferase. FT /FTId=PRO_0000334712. SQ SEQUENCE 172 AA; 19116 MW; 84092A08235F70DD CRC64; MNLKEHIRVI ENFPKEGISF KDVTTILQDG KVLNYTVDKL AENLKDKKID KIVGPEARGF LFGTPLAYKL GVGFVPVRKK GKLPYETISC KYDLEYGQDE LQIHKDSIKK GDKVAIVDDL LATGGTIASV VKLVEELGGE VVNVSFVIEL TDLKGKDKLE GYDINSLVQY NI //