ID   COAE_THEFY              Reviewed;         200 AA.
AC   Q47QN9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 104.
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=Tfu_1192;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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   -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00376}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ55230.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000088; AAZ55230.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q47QN9; -.
DR   SMR; Q47QN9; -.
DR   STRING; 269800.Tfu_1192; -.
DR   EnsemblBacteria; AAZ55230; AAZ55230; Tfu_1192.
DR   KEGG; tfu:Tfu_1192; -.
DR   eggNOG; COG0237; Bacteria.
DR   HOGENOM; CLU_057180_1_1_11; -.
DR   UniPathway; UPA00241; UER00356.
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; 3.40.50.300; -; 1.
DR   HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01121; CoaE; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..200
FT                   /note="Dephospho-CoA kinase"
FT                   /id="PRO_0000243358"
FT   DOMAIN          3..200
FT                   /note="DPCK"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   BINDING         11..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
SQ   SEQUENCE   200 AA;  21881 MW;  26D293F0C0075444 CRC64;
     MLKVGLTGGI GSGKSSVARR LAAHGALVID ADAIAREVVE PGTPALAEIV AEFGDQVLTP
     EGRLDRARLG EIVFADETKL ARLNAIVHPR VGERTQELMA QAKEGTIVVY DVPLLVENNL
     ADQYDVVIVV DVPVHTQVER VTANRGMPEE QVRARINAQA SREQRRAVAD IIIDNSGTEE
     ELDARVAEVW EELQRRLHSR