ID   COAE_PRB01              Reviewed;         197 AA.
AC   Q9F7L5;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 70.
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};
OS   Gamma-proteobacterium EBAC31A08.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples.
OX   NCBI_TaxID=133804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10988064; DOI=10.1126/science.289.5486.1902;
RA   Beja O., Aravind L., Koonin E.V., Suzuki M.T., Hadd A., Nguyen L.P.,
RA   Jovanovich S.B., Gates C.M., Feldman R.A., Spudich J.L., Spudich E.N.,
RA   DeLong E.F.;
RT   "Bacterial rhodopsin: evidence for a new type of phototrophy in the sea.";
RL   Science 289:1902-1906(2000).
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   ---------------------------------------------------------------------------
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; AF279106; AAG10504.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F7L5; -.
DR   SMR; Q9F7L5; -.
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..197
FT                   /note="Dephospho-CoA kinase"
FT                   /id="PRO_0000172976"
FT   DOMAIN          2..197
FT                   /note="DPCK"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT   BINDING         10..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
SQ   SEQUENCE   197 AA;  22017 MW;  8199E3D9BBEAEE7A CRC64;
     MIIGLTGGIG SGKSAAADFF IDLGISVLDA DQVAKEALST NSPGYTDFIS QFGEVYLNNN
     REVDRLKLRE LIFSNPSKKK DLENIIHPIV RSAISNFIIT STSPYSIVMV PLIFETNSYK
     NYDKIITVDC DLELQIVRAS SRDAQNKSQI KNIINKQASR EERLSISDDV LINNSTLSDL
     KKQVNVLHTK YMELLNE