ID E7MMI4_9FIRM Unreviewed; 203 AA.
AC E7MMI4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:EFW24722.1};
GN ORFNames=HMPREF9430_00751 {ECO:0000313|EMBL:EFW24722.1};
OS Solobacterium moorei F0204.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Solobacterium.
OX NCBI_TaxID=706433 {ECO:0000313|EMBL:EFW24722.1, ECO:0000313|Proteomes:UP000004097};
RN [1] {ECO:0000313|EMBL:EFW24722.1, ECO:0000313|Proteomes:UP000004097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0204 {ECO:0000313|EMBL:EFW24722.1,
RC ECO:0000313|Proteomes:UP000004097};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFW24722.1}.
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DR EMBL; AECQ01000012; EFW24722.1; -; Genomic_DNA.
DR RefSeq; WP_006525587.1; NZ_GL637653.1.
DR AlphaFoldDB; E7MMI4; -.
DR STRING; 706433.HMPREF9430_00751; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_0_0_9; -.
DR OrthoDB; 9812943at2; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000004097; 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:EFW24722.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000004097};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:EFW24722.1}.
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 203 AA; 23264 MW; 5622AFB00C0EA8D4 CRC64;
MKIAITGTIA AGKTTVAILF RRRGIPVFNA DQYAKRSLYQ GSVCYEKIRE IFGEDVIGIS
GDIEPKKLAG IIFQDNNKRK QLNAIVHPFV LEGMQKFFAT NHHQPIICAE IPLLFETGWD
QYFDRTVVVT CSEEIAIQRM MEERNYTRQE AKARLSMQIP AEEQIARADK VIYNEGDLKE
LDSQINRWLG ELRKDIRNGK NAN
//
