ID   COAE_MYCTO              Reviewed;         407 AA.
AC   P9WPA2; L0T8U1; O06148; P63826;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
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=MT1667;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK45937.1; -; Genomic_DNA.
DR   PIR; E70559; E70559.
DR   RefSeq; WP_003408069.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPA2; -.
DR   SMR; P9WPA2; -.
DR   EnsemblBacteria; AAK45937; AAK45937; MT1667.
DR   KEGG; mtc:MT1667; -.
DR   PATRIC; fig|83331.31.peg.1790; -.
DR   HOGENOM; CLU_067032_0_0_11; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000001020; 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; Transferase.
FT   CHAIN           1..407
FT                   /note="Dephospho-CoA kinase"
FT                   /id="PRO_0000426987"
FT   DOMAIN          3..204
FT                   /note="DPCK"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   REGION          196..407
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   407 AA;  44669 MW;  166F7A3052943DD7 CRC64;
     MLRIGLTGGI GAGKSLLSTT FSQCGGIVVD GDVLAREVVQ PGTEGLASLV DAFGRDILLA
     DGALDRQALA AKAFRDDESR GVLNGIVHPL VARRRSEIIA AVSGDAVVVE DIPLLVESGM
     APLFPLVVVV HADVELRVRR LVEQRGMAEA DARARIAAQA SDQQRRAVAD VWLDNSGSPE
     DLVRRARDVW NTRVQPFAHN LAQRQIARAP ARLVPADPSW PDQARRIVNR LKIACGHKAL
     RVDHIGSTAV SGFPDFLAKD VIDIQVTVES LDVADELAEP LLAAGYPRLE HITQDTEKTD
     ARSTVGRYDH TDSAALWHKR VHASADPGRP TNVHLRVHGW PNQQFALLFV DWLAANPGAR
     EDYLTVKCDA DRRADGELAR YVTAKEPWFL DAYQRAWEWA DAVHWRP