ID D7GER9_PROFC Unreviewed; 222 AA.
AC D7GER9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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:CBL57030.1};
GN OrderedLocusNames=PFREUD_15310 {ECO:0000313|EMBL:CBL57030.1};
OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL57030.1, ECO:0000313|Proteomes:UP000000936};
RN [1] {ECO:0000313|EMBL:CBL57030.1, ECO:0000313|Proteomes:UP000000936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1
RC {ECO:0000313|Proteomes:UP000000936};
RX PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA Lortal S.;
RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT actinobacterium with food and probiotic applications.";
RL PLoS ONE 5:E11748-E11748(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; FN806773; CBL57030.1; -; Genomic_DNA.
DR RefSeq; WP_013161397.1; NC_014215.1.
DR AlphaFoldDB; D7GER9; -.
DR STRING; 754252.PFREUD_15310; -.
DR KEGG; pfr:PFREUD_15310; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_1_1_11; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000000936; 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:CBL57030.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000000936};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:CBL57030.1}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 222 AA; 23790 MW; AA85163E870D6ED6 CRC64;
MATNPASGAP RKPARDTRQR SHPGQTLVGL TGGIASGKSV VAGMLTDCGA VVIDHDRLAH
DVVDVGTPGL QAVVRRFGDG VLTPDRALNR SRLGAIIFGD ARARHDLDAI IHPLVWKASD
ELEDRAPADA VVVHDVPLLV ETGQQDDFDL VVVVDVPEPL QLRRLIVRNR LSRQQALARI
GAQASRAERL AAADVVIDNS GSLDATRTQV DTLWRRLTGD GH
//
