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Entry: A0A109RDJ9_9LACT
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ID   A0A109RDJ9_9LACT        Unreviewed;       205 AA.
AC   A0A109RDJ9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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   ORFNames=AWM72_06880 {ECO:0000313|EMBL:AMB94491.1};
OS   Aerococcus sanguinicola.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX   NCBI_TaxID=119206 {ECO:0000313|EMBL:AMB94491.1, ECO:0000313|Proteomes:UP000069912};
RN   [1] {ECO:0000313|EMBL:AMB94491.1, ECO:0000313|Proteomes:UP000069912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG43001 {ECO:0000313|EMBL:AMB94491.1,
RC   ECO:0000313|Proteomes:UP000069912};
RX   PubMed=27103727;
RA   Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA   Christensen J.J.;
RT   "Complete Genome Sequences of Aerococcus christensenii CCUG 28831T,
RT   Aerococcus sanguinicola CCUG 43001T, Aerococcus urinae CCUG 36881T,
RT   Aerococcus urinaeequi CCUG 28094T, Aerococcus urinaehominis CCUG 42038 BT,
RT   and Aerococcus viridans CCUG 4311T.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|Proteomes:UP000069912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG43001 {ECO:0000313|Proteomes:UP000069912};
RA   Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA   Christensen J.J.;
RT   "Six Aerococcus type strain genome sequencing and assembly using PacBio and
RT   Illumina Hiseq.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-
CC       Rule:MF_00376}.
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DR   EMBL; CP014160; AMB94491.1; -; Genomic_DNA.
DR   RefSeq; WP_067975285.1; NZ_CP014160.1.
DR   AlphaFoldDB; A0A109RDJ9; -.
DR   KEGG; asan:AWM72_06880; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000069912; 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}; Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:AMB94491.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000069912};
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   205 AA;  23184 MW;  036E976351BCE0E6 CRC64;
     MTFHLGLTGS IATGKSSVSK HFQSLGYPIV DADLGSRAVV EPGQPGLEAI REHFGEDYIF
     PNQTINRKKI GQLIFADDRA RQELNQLLQP HIRQWIIQEA QAYDAAGHEL VVLDIPLLYE
     EGYQEDCDQV MVVYCSESVQ LERLMARDQL SEGEAFQRIC SQISIERKAE WADILIDNGR
     DLSYTYQQLD AWLGISGFRP NPVAE
//
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