ID   COAE_EHRCJ              Reviewed;         200 AA.
AC   Q3YSI1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Dephospho-CoA kinase;
DE            EC=2.7.1.24;
DE   AltName: Full=Dephosphocoenzyme A kinase;
GN   Name=coaE; OrderedLocusNames=Ecaj_0277;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16707693; DOI=10.1128/JB.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P.,
RA   Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C.,
RA   Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W.,
RA   Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
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; CP000107; AAZ68324.1; -; Genomic_DNA.
DR   RefSeq; YP_302922.1; -.
DR   GeneID; 3617662; -.
DR   GenomeReviews; CP000107_GR; Ecaj_0277.
DR   KEGG; ecn:Ecaj_0277; -.
DR   HOGENOM; Q3YSI1; -.
DR   OMA; Q3YSI1; MDAVACV.
DR   BioCyc; ECAN269484:ECAJ_0277-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    200       Dephospho-CoA kinase.
FT                                /FTId=PRO_0000243283.
FT   DOMAIN        3    200       DPCK.
FT   NP_BIND       8     15       ATP (Potential).
SQ   SEQUENCE   200 AA;  23310 MW;  20BBBAEEF65718C0 CRC64;
     MVIFGLTGGI GSGKSLVASY FSTFFKAKIF DADKVVHELY KYDSDVIRLV SEYFPDSVDN
     GIVDRNNLRQ HFLTDNHLWV EFQSVIHAIV LKKKKDFIML HNRRSVRYVV LDIPLLIESN
     FYSCCDFIIH VTTSRLLQMQ RVLRRGLSIK EFESIRCKQL SESSRKKFAN FTIRTGLSKK
     DILFQIKKIM LNVNNKCNMD
//