ID D5GYW7_LACCS Unreviewed; 200 AA.
AC D5GYW7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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:CBL50976.1};
GN OrderedLocusNames=LCRIS_01529 {ECO:0000313|EMBL:CBL50976.1};
OS Lactobacillus crispatus (strain ST1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=748671 {ECO:0000313|EMBL:CBL50976.1, ECO:0000313|Proteomes:UP000002371};
RN [1] {ECO:0000313|EMBL:CBL50976.1, ECO:0000313|Proteomes:UP000002371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST1 {ECO:0000313|EMBL:CBL50976.1,
RC ECO:0000313|Proteomes:UP000002371};
RX PubMed=20435723; DOI=10.1128/JB.00399-10;
RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P.,
RA Edelman S., Westerlund-Wikstrom B., Korhonen T.K., Paulin L., Kankainen M.;
RT "Genome sequence of Lactobacillus crispatus ST1.";
RL J. Bacteriol. 192:3547-3548(2010).
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; FN692037; CBL50976.1; -; Genomic_DNA.
DR RefSeq; WP_013086689.1; NC_014106.1.
DR AlphaFoldDB; D5GYW7; -.
DR KEGG; lcr:LCRIS_01529; -.
DR PATRIC; fig|748671.3.peg.1503; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_0_0_9; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000002371; 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:CBL50976.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; 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 200 AA; 22829 MW; 79C0D83A1FBC2243 CRC64;
MSYVLALTGG IATGKSTADQ FFKANKIPVI DDDQIAHDLM EPGQASWQAI KDYFGSEYLN
DDQTINRKKL GQLVFKDSRA LTKLNELTHP LIFLQTKKLL NQYQAQPIVI LDVPLYFESG
MDKKDIADGV LVITLPEKMQ LQRLKERNHL TDEEARIRMR SQLPMVKKEQ LADFVIENTG
TIKELENKLA QLLVKIREEG
//
