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Database: UniProt
Entry: F0KLA5_ACICP
LinkDB: F0KLA5_ACICP
Original site: F0KLA5_ACICP 
ID   F0KLA5_ACICP            Unreviewed;       198 AA.
AC   F0KLA5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Dephospho-CoA kinase {ECO:0000256|HAMAP-Rule:MF_00376};
DE            EC=2.7.1.24 {ECO:0000256|HAMAP-Rule:MF_00376};
DE   AltName: Full=Dephosphocoenzyme A kinase {ECO:0000256|HAMAP-Rule:MF_00376};
GN   Name=coaE {ECO:0000256|HAMAP-Rule:MF_00376,
GN   ECO:0000313|EMBL:ADY83822.1};
GN   OrderedLocusNames=BDGL_003236 {ECO:0000313|EMBL:ADY83822.1};
OS   Acinetobacter calcoaceticus (strain PHEA-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY83822.1, ECO:0000313|Proteomes:UP000007477};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PHEA-2;
RA   Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.;
RT   "The genome sequence of a nonpathogenic wastewater-adapted bacterium
RT   Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into
RT   environmental adaptation.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY83822.1, ECO:0000313|Proteomes:UP000007477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY83822.1,
RC   ECO:0000313|Proteomes:UP000007477};
RX   PubMed=21441526; DOI=10.1128/JB.00261-11;
RA   Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA   Yuan M., Zhou Z., Elmerich C., Lin M.;
RT   "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT   industry wastewater.";
RL   J. Bacteriol. 193:2672-2673(2011).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC       dephosphocoenzyme A to form coenzyme A. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00376};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 5/5. {ECO:0000256|HAMAP-Rule:MF_00376}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376}.
CC   -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000256|ARBA:ARBA00009018,
CC       ECO:0000256|HAMAP-Rule:MF_00376}.
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DR   EMBL; CP002177; ADY83822.1; -; Genomic_DNA.
DR   RefSeq; WP_002115011.1; NC_016603.1.
DR   RefSeq; YP_004997504.1; NC_016603.1.
DR   AlphaFoldDB; F0KLA5; -.
DR   STRING; 871585.BDGL_003236; -.
DR   GeneID; 11637894; -.
DR   KEGG; acc:BDGL_003236; -.
DR   PATRIC; fig|871585.3.peg.3231; -.
DR   eggNOG; COG0237; Bacteria.
DR   HOGENOM; CLU_057180_1_2_6; -.
DR   OrthoDB; 9812943at2; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000007477; Chromosome.
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   CDD; cd02022; DPCK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR   PANTHER; PTHR10695:SF46; DEPHOSPHO-COA KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10695; DEPHOSPHO-COA KINASE-RELATED; 1.
DR   Pfam; PF01121; CoaE; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00376};
KW   Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:ADY83822.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000007477};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00376}.
FT   BINDING         12..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ   SEQUENCE   198 AA;  22526 MW;  60CE6C6E7A35BA1A CRC64;
     MAFILGVTGG IGSGKSAATQ WFESQGIQVV DADIVAREVV EKGQPALQKI QQTFGDWVLQ
     PDGNLDRRAL REYIFQNPEA RQILEKITHP AIRQSIVQQL QNPKSPYVIL VSPLLFETNQ
     HELVNHTLLV DASEQTQIQR ASQRDGQNQE QIQKIIAAQM PRERKRELAN DIVFNDGLLE
     HLYQQLEPLH QSYLKRAN
//
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