ID I0RVQ5_MYCXE Unreviewed; 406 AA.
AC I0RVQ5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:EID15208.1};
GN ORFNames=MXEN_07951 {ECO:0000313|EMBL:EID15208.1};
OS Mycobacterium xenopi RIVM700367.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID15208.1, ECO:0000313|Proteomes:UP000003584};
RN [1] {ECO:0000313|EMBL:EID15208.1, ECO:0000313|Proteomes:UP000003584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIVM700367 {ECO:0000313|EMBL:EID15208.1,
RC ECO:0000313|Proteomes:UP000003584};
RX PubMed=22628510; DOI=10.1128/JB.00482-12;
RA Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA van Soolingen D., Bitter W., Pain A.;
RT "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL J. Bacteriol. 194:3282-3283(2012).
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:EID15208.1}.
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DR EMBL; AJFI01000038; EID15208.1; -; Genomic_DNA.
DR RefSeq; WP_003920385.1; NZ_AJFI01000038.1.
DR AlphaFoldDB; I0RVQ5; -.
DR PATRIC; fig|1150591.3.peg.1607; -.
DR OrthoDB; 9812943at2; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000003584; 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:EID15208.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000003584};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:EID15208.1}.
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 406 AA; 44111 MW; 6F81D8AA3F51A64D CRC64;
MLRIGLTGGI GAGKSAVTAT FQQCGGIVID ADVIAREVVE PGTEGLAALV NVFGDDILLP
DGSLNRQALA AKAFQNDDTR KTLNGIVHPL VAKRREEIIA AVPDDAVVVE DIPLLVESGM
APLFPLVVVV HADAELRVRR LVEQRGMAED DVRARIAAQA SDEQRRAVAD IWLDNSGSMA
VLAQRASNVW NHRIAPFARN LTARQAVRQP VRLTPADPTW PEQARRIVAR LLAACGGKAL
RVDHIGSTAV PGLDAKDAID IQVTVESLAV ADELADALLS AGYPRIDDIR SDIAKPDPRS
TVAQHDHSYD AALWHKRVHG SADPGRPTYV HVRVDGWPNQ QFALLFVDWL TANPDALAEY
LTVKQKAAAS LPADGSIAEY NEAKEPWLRD AYRRAWNWAE SIGWRP
//
