ID COAA_CORGL Reviewed; 312 AA. AC Q8NRQ2; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 45. DE RecName: Full=Pantothenate kinase; DE EC=2.7.1.33; DE AltName: Full=Pantothenic acid kinase; GN Name=coaA; OrderedLocusNames=Cgl0995, cg1132; OS Corynebacterium glutamicum (Brevibacterium flavum). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1718; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RA Nakagawa S.; RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX MEDLINE=22830012; 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 -!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'- CC phosphopantothenate. 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; BA000036; BAB98388.1; -; Genomic_DNA. DR EMBL; BX927151; CAF19699.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_600220.1; -. DR RefSeq; YP_225285.1; -. DR HSSP; P15044; 1ESM. DR GeneID; 1018982; -. DR GeneID; 3342901; -. DR GenomeReviews; BA000036_GR; Cgl0995. DR GenomeReviews; BX927147_GR; cg1132. DR KEGG; cgb:cg1132; -. DR KEGG; cgl:NCgl0953; -. DR HOGENOM; Q8NRQ2; -. DR OMA; Q8NRQ2; PKVDLIT. DR BioCyc; CGLU196627-1:CG1132-MON; -. DR BRENDA; 2.7.1.33; 812. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 PANTHER; PTHR10285:SF7; PanK_bact; 1. DR PIRSF; PIRSF000545; Pantothenate_kin; 1. DR TIGRFAMs; TIGR00554; panK_bact; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Transferase. FT CHAIN 1 312 Pantothenate kinase. FT /FTId=PRO_0000194424. FT NP_BIND 97 104 ATP (Potential). SQ SEQUENCE 312 AA; 35316 MW; BBDE9EF3C83F95F6 CRC64; MKPSPRTPDF SPYLDFDRAQ WRELRNSMPQ VLTQKEVIEL RGIGENIDLA EVAEVYLPLS RLIHLQVAAR QQLTAATETF LGTSPSISVP FVIGVAGSVA VGKSTTARLL QVLLQRWNSH PRVDLVTTDG FLYPGAELIR RGLMSRKGFP ESYDQRALLR FVTDVKSGKL EVNAPVYSHT AYDRVPGEFT TVRQPDILIV EGLNVLQTGP TLMVSDLFDF SVYVDARTED IEKWYIDRFL KLRDTAFRRP GAHFSHYADM ADPESIAVAR ELWQSINLPN LVENILPTRV RASLVLKKGS DHLVERVRMR KI //