ID COAE_BURTA Reviewed; 203 AA. AC Q2SZG8; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, 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=BTH_I1133; OS Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / OS CIP 106301). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., RA Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., RA Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., RA Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., RA Roberts K., Hatch B., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. 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; CP000086; ABC39050.1; -; Genomic_DNA. DR RefSeq; YP_441681.1; -. DR GeneID; 3847692; -. DR GenomeReviews; CP000086_GR; BTH_I1133. DR KEGG; bte:BTH_I1133; -. DR TIGR; BTH_I1133; -. DR HOGENOM; Q2SZG8; -. DR OMA; Q2SZG8; LHPMIRQ. DR BioCyc; BTHA271848:BTH_I1133-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 1 203 Dephospho-CoA kinase. FT /FTId=PRO_0000243270. FT DOMAIN 3 201 DPCK. FT NP_BIND 8 15 ATP (Potential). SQ SEQUENCE 203 AA; 21731 MW; D07A34CAAD90DB88 CRC64; MFSVGLTGGI GSGKTTVSNL FGALGATIVD TDLIAHRITA PHGLAMPFIE REFGAQFVAA DGSLDRAKMR ALIFSDESAR KRLEAITHPL IREETEREAG AAHGAYVVFV VPLLVESGTW EARVDRVLVV DCDVETQIAR VMSRNGFARE QVEAIVARQA SRDARLAAAD DVIVNDNASL DELAAEVAAL HQRYLGYAAA APN //