ID S2WHX3_9ACTN Unreviewed; 208 AA.
AC S2WHX3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=HMPREF9306_01775 {ECO:0000313|EMBL:EPD32207.1};
OS Propionimicrobium lymphophilum ACS-093-V-SCH5.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionimicrobium.
OX NCBI_TaxID=883161 {ECO:0000313|EMBL:EPD32207.1, ECO:0000313|Proteomes:UP000014417};
RN [1] {ECO:0000313|EMBL:EPD32207.1, ECO:0000313|Proteomes:UP000014417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-093-V-SCH5 {ECO:0000313|EMBL:EPD32207.1,
RC ECO:0000313|Proteomes:UP000014417};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Propionimicrobium lymphophilum ACS-093-V-SCH5.";
RL Submitted (APR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPD32207.1}.
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DR EMBL; AGZR01000009; EPD32207.1; -; Genomic_DNA.
DR AlphaFoldDB; S2WHX3; -.
DR STRING; 883161.HMPREF9306_01775; -.
DR PATRIC; fig|883161.3.peg.1764; -.
DR HOGENOM; CLU_057180_1_1_11; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000014417; Unassembled WGS sequence.
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:EPD32207.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000014417};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00376}.
FT BINDING 24..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 208 AA; 22970 MW; 16F3390CA2D9A2EA CRC64;
MSEISESLRY GAHMLKVGLT GGIASGKTSV ANQLRDLGAT IIDSDVLARE VVEPGTDGFA
EVVKRFGNRA IGPDGGLDRQ WLGSVVFLDE NARRDLNAII HPRVRKAARL MEAQVPDDGV
AVQVIPLLVE TNQQDDFDCV VVVDVPEEVQ IKRLVARNGF TRPQAESRIR SQASRQERLA
VADFVIDNSS SFEHTRIQVE ELWRRLVG
//
