ID COAE_BURPS STANDARD; PRT; 203 AA. AC Q9ZF69; Q63QL2; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 2. DT 07-MAR-2006, entry version 38. DE Dephospho-CoA kinase (EC 2.7.1.24) (Dephosphocoenzyme A kinase). GN Name=coaE; OrderedLocusNames=BPSL3011; OS Burkholderia pseudomallei (Pseudomonas pseudomallei). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=28450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., RA Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A., RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, RT Burkholderia pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57. RC STRAIN=1026b; RX MEDLINE=99350433; PubMed=10419967; RA DeShazer D., Brett P.J., Burtnick M.N., Woods D.E.; RT "Molecular characterization of genetic loci required for secretion of RT exoproducts in Burkholderia pseudomallei."; RL J. Bacteriol. 181:4661-4664(1999). CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group CC of dephosphocoenzyme A to form coenzyme A (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + dephospho-CoA = ADP + CoA. CC -!- PATHWAY: Coenzyme A (CoA) biosynthesis; fifth (last) step. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the coaE 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; BX571965; CAH37022.1; -; Genomic_DNA. DR EMBL; AF110186; AAD05190.1; -; Genomic_DNA. DR HSSP; P44920; 1JJV. DR GenomeReviews; BX571965_GR; BPSL3011. 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; PS01294; COAE; 1. KW ATP-binding; Coenzyme A biosynthesis; Complete proteome; Kinase; KW Nucleotide-binding; Transferase. FT CHAIN 1 203 Dephospho-CoA kinase. FT /FTId=PRO_0000172921. FT NP_BIND 8 15 ATP (Potential). SQ SEQUENCE 203 AA; 21719 MW; D0E6CF8FF02B9853 CRC64; MFSVGLTGGI GSGKTTVADL FGKLGATIVD TDLIAHRITA PQGLAMPLIA REFGAEFVAA DGSLDRAKMR ALVFSDESAR KRLEAITHPL IREETEREAR TAQGAYVVFV VPLLVESGTW KTRVDRVLVV DCDVETQIAR VTARNGFTRA QVEAIVARQA SRDARLAAAD DVIANDNASV AELAAEVAAL HQRYLECAAA ARN //