ID   DPCKG_PYRHO             Reviewed;         179 AA.
AC   O59572;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=PH1909;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA31034.1; -; Genomic_DNA.
DR   PIR; C71205; C71205.
DR   RefSeq; WP_010885974.1; NC_000961.1.
DR   AlphaFoldDB; O59572; -.
DR   STRING; 70601.3258351; -.
DR   EnsemblBacteria; BAA31034; BAA31034; BAA31034.
DR   GeneID; 1442756; -.
DR   KEGG; pho:PH1909; -.
DR   eggNOG; arCOG04076; Archaea.
DR   OMA; AIYDHKT; -.
DR   OrthoDB; 116732at2157; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000000752; 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; Transferase.
FT   CHAIN           1..179
FT                   /note="GTP-dependent dephospho-CoA kinase"
FT                   /id="PRO_0000137616"
SQ   SEQUENCE   179 AA;  19945 MW;  4CCE93EEE31D2648 CRC64;
     MRVVFKLPDE LRQELKNPLG ELIEGNIPEP YVKAKNIIEG DDGVLITVGD VVTENIMRVG
     LNPNLAIYDH KTERREYKPR IIINGVLLTV KNPPGTITLP LLKSIKKAYS LILNGKSVHI
     VVNGEEDLAT IPAVLYAPLG ATVIYGQPKR GIVLIKVTNE CKRRCAKIMR RMEVVRDGD