COAE_VIBVU
ID COAE_VIBVU Reviewed; 202 AA.
AC Q56741;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 130.
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=VV1_1622, VV1_1621;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MO6-24;
RA Strom M.S., Lara J.C.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION.
RC STRAIN=CMCP6;
RX PubMed=21245845; DOI=10.1038/msb.2010.115;
RA Kim H.U., Kim S.Y., Jeong H., Kim T.Y., Kim J.J., Choy H.E., Yi K.Y.,
RA Rhee J.H., Lee S.Y.;
RT "Integrative genome-scale metabolic analysis of Vibrio vulnificus for drug
RT targeting and discovery.";
RL Mol. Syst. Biol. 7:460-460(2011).
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, ECO:0000305}.
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DR EMBL; U48808; AAA91207.1; -; Genomic_DNA.
DR EMBL; AE016795; AAO10041.2; -; Genomic_DNA.
DR RefSeq; WP_011079547.1; NC_004459.3.
DR AlphaFoldDB; Q56741; -.
DR SMR; Q56741; -.
DR EnsemblBacteria; AAO10041; AAO10041; VV1_1622.
DR KEGG; vvu:VV1_1622; -.
DR HOGENOM; CLU_057180_1_2_6; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000002275; 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..202
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000173029"
FT DOMAIN 4..201
FT /note="DPCK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT CONFLICT 79
FT /note="S -> A (in Ref. 1; AAA91207)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="S -> G (in Ref. 1; AAA91207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22555 MW; 147278671EBB75C1 CRC64;
MALVIGLTGG IASGKTTVAN LFQQHFAIDI VDADIVARQV VAPGSAGLAA IVDHFGADIL
TCEGELDRGQ LRQRIFAHSE EKQWLNALLH PMIRRKMIED LAQVSSPYAL LVVPLLVENQ
LQTLCDRVLV VDVEEKTQLQ RTMDRDSVDE QQVRAILKAQ ASRHERLALA DDVIKNESKD
QDLLQQITDL HQKYLAMSKQ NR