ID A0A448I5X1_MYCCI Unreviewed; 396 AA.
AC A0A448I5X1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:VEG47760.1};
GN ORFNames=NCTC10485_02047 {ECO:0000313|EMBL:VEG47760.1};
OS Mycolicibacterium chitae (Mycobacterium chitae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1792 {ECO:0000313|EMBL:VEG47760.1, ECO:0000313|Proteomes:UP000282551};
RN [1] {ECO:0000313|EMBL:VEG47760.1, ECO:0000313|Proteomes:UP000282551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10485 {ECO:0000313|EMBL:VEG47760.1,
RC ECO:0000313|Proteomes:UP000282551};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00376}.
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DR EMBL; LR134355; VEG47760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448I5X1; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000282551; Chromosome 1.
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:VEG47760.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000282551};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:VEG47760.1}.
SQ SEQUENCE 396 AA; 43553 MW; 0BED3C752E5A6482 CRC64;
MSATFTECGG IVVDGDVIAR EVVEPGTEGL AKLVDAFGRD ILHDSGPQAG ALNRPALAAI
AFSDDDKRAT LNGIVHPLVA HRRSELIAAA VEAHESPVII EDIPLLVESQ MAPMFPLVII
VHAEVETRVA RLMEHRGFSE EDARARIAAQ ATEEQRRAVA DVWLDNSGTA GDLKERARAL
WHERILPFSH NLQHREPARA EVRLVPSDPS WPAQAARIVN RLNTAGGHRV RRIDHIGSTA
VPGLDAKDVI DIQVTVDSLA TADELTEGLL AAGYLRLENI TADVPKPNGR STVGEFDHTD
DASLWRKRYF KSADPGRPTN VHVRVDGWPN QQFALLFTDW IAANPGVQAD YLAAKRHAHE
RGGGDIGAYA EAKEPWFLDA YRRAWEWADT TGWRPR
//
