ID COAA_ECOLI Reviewed; 316 AA. AC P0A6I3; P15044; Q2M8R5; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 1. DT 05-FEB-2008, entry version 36. DE Pantothenate kinase (EC 2.7.1.33) (Pantothenic acid kinase) (Rts DE protein). GN Name=coaA; Synonyms=panK, rts; OrderedLocusNames=b3974, JW3942; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93015690; PubMed=1328157; RA Song W.-J., Jackowski S.; RT "Cloning, sequencing, and expression of the pantothenate kinase (coaA) RT gene of Escherichia coli."; RL J. Bacteriol. 174:6411-6417(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92165753; PubMed=1311303; RA Song W.-J., Jackowski S.; RT "coaA and rts are allelic and located at kilobase 3532 on the RT Escherichia coli physical map."; RL J. Bacteriol. 174:1705-1706(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89232747; PubMed=3073109; DOI=10.1016/0378-1119(88)90189-8; RA Flamm J.A., Friesen J.D., Otsuka A.J.; RT "The nucleotide sequence of the Escherichia coli rts gene."; RL Gene 74:555-558(1988). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=94089392; PubMed=8265357; DOI=10.1093/nar/21.23.5408; RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., RA Daniels D.L.; RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the RT region from 89.2 to 92.8 minutes."; RL Nucleic Acids Res. 21:5408-5417(1993). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'- CC phosphopantothenate. CC -!- ENZYME REGULATION: Regulated by feedback inhibition by CoA and its CC thioesters. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; coenzyme CC A from pantothenate: step 1/5. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family. 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; M36321; AAA76838.1; ALT_INIT; Genomic_DNA. DR EMBL; M90071; AAA23590.1; -; Genomic_DNA. DR EMBL; M90071; AAA23591.1; ALT_INIT; Genomic_DNA. DR EMBL; U00006; AAC43076.1; -; Genomic_DNA. DR EMBL; U00096; AAC76952.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77341.1; -; Genomic_DNA. DR PIR; A45727; BVECRS. DR RefSeq; AP_003840.1; -. DR RefSeq; NP_418405.1; -. DR PDB; 1ESM; X-ray; 2.50 A; A/B/C/D=1-316. DR PDB; 1ESN; X-ray; 2.60 A; A/B/C/D=1-316. DR PDB; 1SQ5; X-ray; 2.20 A; A/B/C/D=9-316. DR PDBsum; 1ESM; -. DR PDBsum; 1ESN; -. DR PDBsum; 1SQ5; -. DR IntAct; P0A6I3; -. DR GeneID; 948479; -. DR GenomeReviews; U00096_GR; b3974. DR GenomeReviews; AP009048_GR; JW3942. DR KEGG; ecj:JW3942; -. DR KEGG; eco:b3974; -. DR EchoBASE; EB0915; -. DR EcoGene; EG10922; coaA. DR BioCyc; EcoCyc:PANTOTHENATE-KIN-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004594; F:pantothenate kinase activity; IEA:HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00215; -; 1. DR InterPro; IPR004566; PanK_bact. DR InterPro; IPR006083; PRK_URK. DR Pfam; PF00485; PRK; 1. DR PIRSF; PIRSF000545; Pantothenate_kin; 1. DR TIGRFAMs; TIGR00554; panK_bact; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Complete proteome; KW Cytoplasm; Kinase; Nucleotide-binding; Transferase. FT CHAIN 1 316 Pantothenate kinase. FT /FTId=PRO_0000194426. FT NP_BIND 95 102 ATP (Potential). FT STRAND 11 16 FT HELIX 17 22 FT HELIX 33 42 FT HELIX 48 53 FT HELIX 55 80 FT STRAND 89 95 FT HELIX 101 112 FT STRAND 121 125 FT HELIX 126 129 FT HELIX 133 139 FT HELIX 148 150 FT HELIX 153 163 FT TURN 164 166 FT STRAND 170 172 FT TURN 177 180 FT STRAND 188 190 FT STRAND 195 199 FT TURN 201 204 FT HELIX 207 209 FT HELIX 219 222 FT STRAND 224 230 FT HELIX 233 249 FT TURN 250 253 FT HELIX 260 263 FT HELIX 267 280 FT HELIX 282 288 FT HELIX 291 296 FT STRAND 298 303 FT HELIX 305 307 FT STRAND 309 315 SQ SEQUENCE 316 AA; 36360 MW; DDDC1922C5C52A70 CRC64; MSIKEQTLMT PYLQFDRNQW AALRDSVPMT LSEDEIARLK GINEDLSLEE VAEIYLPLSR LLNFYISSNL RRQAVLEQFL GTNGQRIPYI ISIAGSVAVG KSTTARVLQA LLSRWPEHRR VELITTDGFL HPNQVLKERG LMKKKGFPES YDMHRLVKFV SDLKSGVPNV TAPVYSHLIY DVIPDGDKTV VQPDILILEG LNVLQSGMDY PHDPHHVFVS DFVDFSIYVD APEDLLQTWY INRFLKFREG AFTDPDSYFH NYAKLTKEEA IKTAMTLWKE INWLNLKQNI LPTRERASLI LTKSANHAVE EVRLRK //