ID COAE_COLP3 Reviewed; 202 AA. AC Q47VS4; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 26. DE RecName: Full=Dephospho-CoA kinase; DE EC=2.7.1.24; DE AltName: Full=Dephosphocoenzyme A kinase; GN Name=coaE; OrderedLocusNames=CPS_4450; OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio OS psychroerythus). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Colwelliaceae; Colwellia. OX NCBI_TaxID=167879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16043709; DOI=10.1073/pnas.0504766102; RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B., RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.; RT "The psychrophilic lifestyle as revealed by the genome sequence of RT Colwellia psychrerythraea 34H through genomic and proteomic RT analyses."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005). CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group CC of dephosphocoenzyme A to form coenzyme A (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; coenzyme CC A from pantothenate: step 5/5. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the coaE family. CC -!- SIMILARITY: Contains 1 DPCK (dephospho-CoA kinase) domain. 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; CP000083; AAZ26036.1; -; Genomic_DNA. DR RefSeq; YP_271098.1; -. DR GeneID; 3520284; -. DR GenomeReviews; CP000083_GR; CPS_4450. DR KEGG; cps:CPS_4450; -. DR NMPDR; fig|167879.3.peg.4166; -. DR TIGR; CPS_4450; -. DR HOGENOM; Q47VS4; -. DR OMA; Q47VS4; LHPMIRQ. DR BioCyc; CPSY167879:CPS_4450-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00376; -; 1. DR InterPro; IPR001977; Depp_CoAkinase. DR PANTHER; PTHR10695; Depp_CoAkinase; 1. DR Pfam; PF01121; CoaE; 1. DR ProDom; PD003329; Depp_CoAkinase; 1. DR TIGRFAMs; TIGR00152; Depp_CoAkinase; 1. DR PROSITE; PS51219; DPCK; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Transferase. FT CHAIN 1 202 Dephospho-CoA kinase. FT /FTId=PRO_0000243277. FT DOMAIN 5 202 DPCK. FT NP_BIND 10 17 ATP (Potential). SQ SEQUENCE 202 AA; 22260 MW; 54698B3F2768CF1F CRC64; MSKLVIGLTG GIGSGKTTIT NYFLALGVEI IDADIIAREV VAINSPALKA IAKHFGDDYI QADGQLNRPL LRNRIFSNKA DKLWLNKLLH PLIRVNIVTQ TKEAKSPYCI LVAPLLIENN LLELVDRVLI VDVNESTQIT RTLVRDSSSE QEIKAIIASQ TSRAARVNVA DDIINNDDSP LSEIKEAVLS LDKKYLTLTK MV //