ID   COAE_BURP2              Reviewed;         203 AA.
AC   I1WFB9; Q63QL2; Q9ZF69;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00376};
DE            EC=2.7.1.24 {ECO:0000255|HAMAP-Rule:MF_00376};
DE   AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376};
GN   Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376};
GN   OrderedLocusNames=BP1026B_I0297;
OS   Burkholderia pseudomallei (strain 1026b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=884204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1026b;
RX   PubMed=22615773; DOI=10.1371/journal.pone.0036507;
RA   Hayden H.S., Lim R., Brittnacher M.J., Sims E.H., Ramage E.R., Fong C.,
RA   Wu Z., Crist E., Chang J., Zhou Y., Radey M., Rohmer L., Haugen E.,
RA   Gillett W., Wuthiekanun V., Peacock S.J., Kaul R., Miller S.I., Manoil C.,
RA   Jacobs M.A.;
RT   "Evolution of Burkholderia pseudomallei in recurrent melioidosis.";
RL   PLoS ONE 7:E36507-E36507(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
RC   STRAIN=1026b;
RX   PubMed=10419967; DOI=10.1128/jb.181.15.4661-4664.1999;
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 of
CC       dephosphocoenzyme A to form coenzyme A. {ECO:0000255|HAMAP-
CC       Rule:MF_00376}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+);
CC         Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC         EC=2.7.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00376};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}.
CC   -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00376}.
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DR   EMBL; CP002833; AFI64963.1; -; Genomic_DNA.
DR   EMBL; AF110186; AAD05190.1; -; Genomic_DNA.
DR   RefSeq; WP_004194322.1; NZ_CP004379.1.
DR   AlphaFoldDB; I1WFB9; -.
DR   SMR; I1WFB9; -.
DR   EnsemblBacteria; AFI64963; AFI64963; BP1026B_I0297.
DR   GeneID; 56594269; -.
DR   KEGG; bpz:BP1026B_I0297; -.
DR   PATRIC; fig|884204.3.peg.306; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000010087; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01121; CoaE; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00152; TIGR00152; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..203
FT                   /note="Dephospho-CoA kinase"
FT                   /id="PRO_0000429786"
FT   DOMAIN          3..201
FT                   /note="DPCK"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   BINDING         11..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
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