ID   DPCKG_ARCFU             Reviewed;         186 AA.
AC   O29150;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=GTP-dependent dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00590};
DE            EC=2.7.1.- {ECO:0000255|HAMAP-Rule:MF_00590};
DE   AltName: Full=Dephospho-coenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00590};
DE            Short=DPCK {ECO:0000255|HAMAP-Rule:MF_00590};
GN   OrderedLocusNames=AF_1115;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- FUNCTION: Catalyzes the GTP-dependent phosphorylation of the 3'-
CC       hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
CC       {ECO:0000255|HAMAP-Rule:MF_00590}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA + GTP = CoA + GDP + H(+);
CC         Xref=Rhea:RHEA:61156, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00590};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00590}.
CC   -!- SIMILARITY: Belongs to the GTP-dependent DPCK family.
CC       {ECO:0000255|HAMAP-Rule:MF_00590}.
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DR   EMBL; AE000782; AAB90127.1; -; Genomic_DNA.
DR   PIR; B69389; B69389.
DR   RefSeq; WP_010878611.1; NC_000917.1.
DR   AlphaFoldDB; O29150; -.
DR   STRING; 224325.AF_1115; -.
DR   EnsemblBacteria; AAB90127; AAB90127; AF_1115.
DR   GeneID; 24794720; -.
DR   KEGG; afu:AF_1115; -.
DR   eggNOG; arCOG04076; Archaea.
DR   HOGENOM; CLU_120795_0_0_2; -.
DR   OMA; AIYDHKT; -.
DR   OrthoDB; 116732at2157; -.
DR   PhylomeDB; O29150; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0016301; F: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   HAMAP; MF_00590; Dephospho_CoA_kinase_GTP_dep; 1.
DR   InterPro; IPR007164; GTP-dep_dephospho-CoA_kin.
DR   PANTHER; PTHR40732; PTHR40732; 1.
DR   Pfam; PF04019; DUF359; 1.
DR   PIRSF; PIRSF006533; UCP006533; 1.
PE   3: Inferred from homology;
KW   Coenzyme A biosynthesis; Kinase; Reference proteome; Transferase.
FT   CHAIN           1..186
FT                   /note="GTP-dependent dephospho-CoA kinase"
FT                   /id="PRO_0000137606"
SQ   SEQUENCE   186 AA;  20278 MW;  02AA66E1C5055606 CRC64;
     MKGLRLPESM REELAKPHGK LYRGKGEKLL LEVEEISEAK PFCTVGDLVT ASAIKVGLTP
     DLAVADGKTL REENVEFEQE AFDEVIETTN PPAHISCELI SALLKALKLC EDGKKVLVFV
     DGEEDLAVVP LVKLLPLGAL ILYGQPGEGV VALKVDEEKK VLILNLLNKM EIIGECDELK
     YLLGGD