ID 6PGL_HUMAN Reviewed; 258 AA. AC O95336; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 19-FEB-2014, entry version 116. DE RecName: Full=6-phosphogluconolactonase; DE Short=6PGL; DE EC=3.1.1.31; GN Name=PGLS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10518023; DOI=10.1016/S0014-5793(99)01247-8; RA Collard F., Collet J.-F., Gerin I., Veiga-da-Cunha M., RA van Schaftingen E.; RT "Identification of the cDNA encoding human 6-phosphogluconolactonase, RT the enzyme catalyzing the second step of the pentose phosphate RT pathway."; RL FEBS Lett. 459:223-226(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 41-72 AND 82-96, AND MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-242. RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.; RT "Full-insert sequence of mapped XREF EST."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND RP CLEAVAGE OF INITIATOR METHIONINE. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-180, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate. CC -!- CATALYTIC ACTIVITY: 6-phospho-D-glucono-1,5-lactone + H(2)O = 6- CC phospho-D-gluconate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 2/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase subfamily. CC -!- SEQUENCE CAUTION: CC Sequence=AAC72960.1; Type=Erroneous initiation; 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; AJ243972; CAB57866.1; -; mRNA. DR EMBL; BC014006; AAH14006.1; -; mRNA. DR EMBL; AF091091; AAC72960.1; ALT_INIT; mRNA. DR RefSeq; NP_036220.1; NM_012088.2. DR UniGene; Hs.466165; -. DR ProteinModelPortal; O95336; -. DR SMR; O95336; 38-247. DR BioGrid; 117328; 8. DR MINT; MINT-5000838; -. DR STRING; 9606.ENSP00000252603; -. DR PhosphoSite; O95336; -. DR OGP; O95336; -. DR REPRODUCTION-2DPAGE; IPI00029997; -. DR PaxDb; O95336; -. DR PeptideAtlas; O95336; -. DR PRIDE; O95336; -. DR DNASU; 25796; -. DR Ensembl; ENST00000252603; ENSP00000252603; ENSG00000130313. DR GeneID; 25796; -. DR KEGG; hsa:25796; -. DR UCSC; uc002ngw.3; human. DR CTD; 25796; -. DR GeneCards; GC19P017622; -. DR HGNC; HGNC:8903; PGLS. DR HPA; HPA040744; -. DR HPA; HPA042032; -. DR MIM; 604951; gene. DR neXtProt; NX_O95336; -. DR PharmGKB; PA33240; -. DR eggNOG; COG0363; -. DR HOGENOM; HOG000256285; -. DR HOVERGEN; HBG000030; -. DR InParanoid; O95336; -. DR KO; K01057; -. DR OMA; TYGLYKS; -. DR OrthoDB; EOG7RZ5QV; -. DR PhylomeDB; O95336; -. DR TreeFam; TF318609; -. DR BRENDA; 3.1.1.31; 2681. DR Reactome; REACT_111217; Metabolism. DR UniPathway; UPA00115; UER00409. DR GenomeRNAi; 25796; -. DR NextBio; 46981; -. DR PRO; PR:O95336; -. DR ArrayExpress; O95336; -. DR Bgee; O95336; -. DR CleanEx; HS_PGLS; -. DR Genevestigator; O95336; -. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IDA:UniProtKB. DR GO; GO:0048029; F:monosaccharide binding; IEA:Ensembl. DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:Ensembl. DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB. DR InterPro; IPR006148; Glc/Gal-6P_isomerase. DR Pfam; PF01182; Glucosamine_iso; 1. DR TIGRFAMs; TIGR01198; pgl; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; KW Hydrolase; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 258 6-phosphogluconolactonase. FT /FTId=PRO_0000090078. FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 180 180 N6-acetyllysine. SQ SEQUENCE 258 AA; 27547 MW; A753FB7E662116DD CRC64; MAAPAPGLIS VFSSSQELGA ALAQLVAQRA ACCLAGARAR FALGLSGGSL VSMLARELPA AVAPAGPASL ARWTLGFCDE RLVPFDHAES TYGLYRTHLL SRLPIPESQV ITINPELPVE EAAEDYAKKL RQAFQGDSIP VFDLLILGVG PDGHTCSLFP DHPLLQEREK IVAPISDSPK PPPQRVTLTL PVLNAARTVI FVATGEGKAA VLKRILEDQE ENPLPAALVQ PHTGKLCWFL DEAAARLLTV PFEKHSTL //