COAE_MYCLE
ID COAE_MYCLE Reviewed; 410 AA.
AC Q50178;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00376};
DE EC=2.7.1.24 {ECO:0000255|HAMAP-Rule:MF_00376};
DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376};
GN Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376}; OrderedLocusNames=ML1383;
GN ORFNames=o410;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7476188; DOI=10.1111/j.1365-2958.1995.tb02317.x;
RA Fsihi H., Cole S.T.;
RT "The Mycobacterium leprae genome: systematic sequence analysis identifies
RT key catabolic enzymes, ATP-dependent transport systems and a novel polA
RT locus associated with genomic variability.";
RL Mol. Microbiol. 16:909-919(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC dephosphocoenzyme A to form coenzyme A. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00376};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}.
CC -!- DOMAIN: The C-terminal UPF0157 domain is involved in the proper folding
CC of the full length enzyme. {ECO:0000255|HAMAP-Rule:MF_00376}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CoaE family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the UPF0157 (GrpB)
CC family. {ECO:0000305}.
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DR EMBL; Z46257; CAA86366.1; -; Genomic_DNA.
DR EMBL; AL583921; CAC31764.1; -; Genomic_DNA.
DR PIR; S77661; S77661.
DR RefSeq; NP_301984.1; NC_002677.1.
DR RefSeq; WP_010908305.1; NC_002677.1.
DR AlphaFoldDB; Q50178; -.
DR SMR; Q50178; -.
DR STRING; 272631.ML1383; -.
DR EnsemblBacteria; CAC31764; CAC31764; CAC31764.
DR KEGG; mle:ML1383; -.
DR PATRIC; fig|272631.5.peg.2566; -.
DR Leproma; ML1383; -.
DR eggNOG; COG0237; Bacteria.
DR eggNOG; COG2320; Bacteria.
DR HOGENOM; CLU_067032_0_0_11; -.
DR OMA; IRVDGWP; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000000806; Chromosome.
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 Gene3D; 3.30.460.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF01121; CoaE; 1.
DR Pfam; PF04229; GrpB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..410
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000172963"
FT DOMAIN 3..201
FT /note="DPCK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT REGION 196..410
FT /note="UPF0157"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
SQ SEQUENCE 410 AA; 44976 MW; 923F0408658A6A73 CRC64;
MLCIGITGGI GAGKSLLSST FSQCGGIVVD GDVLAREVVQ PGTKGLSSLV DAFGQDILLP
GGALDRRALA VKAFRDDAAR NVLNGIVHPL VANRRAEIIA AISEDAVVVE DIPLLVESGM
AHLFPLVVVV HADVELRVRR LVEQRGVAET DARARIAAQA SDEERRAVAD VWLDNSSTPE
VLVQRARDLW YHRILPFAYN LSQRQAVYAP AGLVTSDPIW LGQAKRIVAR LKTTCGHKAL
RVDHIGSTAV PHYPGFPDFQ AKDIIDIQIT VESLAMADEL ADPLLSAGYP RLEHVTGDAA
KTNARSTVDR YEHSSDPNLW HKRFHASADP GRPTYVHIRV AGWPNQQFGL LFVDWLKANP
GVRADYLDVK RTADRLAAGD MGRYADAKEP WLLDAYRRAW EWADSTGWRL
