ID A0A0M2JVT0_9MYCO Unreviewed; 401 AA.
AC A0A0M2JVT0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:KKF01178.1};
GN ORFNames=EUA04_19215 {ECO:0000313|EMBL:TDL05954.1}, WN67_15120
GN {ECO:0000313|EMBL:KKF01178.1};
OS Mycolicibacterium obuense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1807 {ECO:0000313|EMBL:KKF01178.1, ECO:0000313|Proteomes:UP000034150};
RN [1] {ECO:0000313|EMBL:KKF01178.1, ECO:0000313|Proteomes:UP000034150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|EMBL:KKF01178.1,
RC ECO:0000313|Proteomes:UP000034150};
RA Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium obuense UC1.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TDL05954.1, ECO:0000313|Proteomes:UP000294952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22DIII {ECO:0000313|EMBL:TDL05954.1,
RC ECO:0000313|Proteomes:UP000294952};
RA Tiago I., Alarico S., Pereira S.G., Coelho C., Maranha A., Empadinhas N.;
RT "High-quality-draft genome sequences of five non-tuberculosis
RT mycobacteriaceae isolated from a nosocomial environment.";
RL Submitted (JAN-2019) 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 -!- SIMILARITY: In the C-terminal section; belongs to the UPF0157 (GrpB)
CC family. {ECO:0000256|ARBA:ARBA00011058}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CoaE family.
CC {ECO:0000256|ARBA:ARBA00008826}.
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:KKF01178.1}.
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DR EMBL; LAUZ02000033; KKF01178.1; -; Genomic_DNA.
DR EMBL; SDLP01000006; TDL05954.1; -; Genomic_DNA.
DR RefSeq; WP_046363865.1; NZ_SDLP01000006.1.
DR STRING; 1807.MOBUDSM44075_03784; -.
DR PATRIC; fig|1807.13.peg.3128; -.
DR OrthoDB; 9812943at2; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000034150; Unassembled WGS sequence.
DR Proteomes; UP000294952; 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; 3.30.460.10; Beta Polymerase, domain 2; 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; IPR007344; GrpB/CoaE.
DR InterPro; IPR043519; NT_sf.
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 Pfam; PF04229; GrpB; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 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};
KW Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:KKF01178.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:KKF01178.1}.
FT REGION 200..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 401 AA; 43359 MW; 1B6CE1DDF5683FDD CRC64;
MLRIGLTGGI GAGKSTVSAT FDELGGIVVD GDVIAREVVE PGTEGLAKLV EAFGEGILAE
DGTLNRPALA AIAFSDEEKR KTLNGIVHPL VGQRRSELIA AAADDAVIIE DIPLLVESHM
APFFPLVIIV HADEEVRVKR LIEHRGFTED DARARIAAQA TEADRRAVAD VWLDNAGTAD
QLKAAARTLW NDRIEPFADN LRAGRPAPTE PRLVPPDPEW PAQAERILAR LRTACGHHAS
RVDHIGSTAV PGLDAKDVID VQVTVASLDV ADDLADALLG AGYVRTEITE DVAKDIAKDT
AKPGVDGQWG KRLYCSADPG RPTNVHVRVD GWPNQRFALL FVDWLTAEPA ARADYLELKR
RVAAEGHATT GDYADAKEPW FADAYRRAWA WADATGWQPP Q
//
