ID   COAE_CHLTE              Reviewed;         208 AA.
AC   Q8KD46;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=Dephospho-CoA kinase;
DE            EC=2.7.1.24;
DE   AltName: Full=Dephosphocoenzyme A kinase;
GN   Name=coaE; OrderedLocusNames=CT1209;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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.
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DR   EMBL; AE006470; AAM72441.1; -; Genomic_DNA.
DR   RefSeq; NP_662099.1; -.
DR   HSSP; P36679; 1N3B.
DR   GeneID; 1006569; -.
DR   GenomeReviews; AE006470_GR; CT1209.
DR   KEGG; cte:CT1209; -.
DR   NMPDR; fig|194439.1.peg.1193; -.
DR   TIGR; CT1209; -.
DR   HOGENOM; Q8KD46; -.
DR   OMA; Q8KD46; NRLVHPK.
DR   BioCyc; CTEP194439:CT_1209-MON; -.
DR   BRENDA; 2.7.1.24; 189605.
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    208       Dephospho-CoA kinase.
FT                                /FTId=PRO_0000172927.
FT   DOMAIN        8    208       DPCK.
FT   NP_BIND      13     20       ATP (Potential).
SQ   SEQUENCE   208 AA;  23057 MW;  7D51E3B49C79741A CRC64;
     MKARLPLLVG VTGGIGSGKS TVCAMLAEMG CELFEADRIA KELQVEDPEV IRGIEKLFGP
     DVYSRDASGK LLIDRKAIAA IVFSEPEKLA ALNRLIHPKV REAFVNEVKR CAREGKRILC
     KEAAILFEAG ADRDLDRIIV VAANDGLRLA RAVARGLACE EARKRMQAQW PQEKLVERAH
     YVIFNDGTLD ELRSQVEQVY QSLLTVVE
//