ID   DPCKG_HALMA             Reviewed;         179 AA.
AC   Q5UYR8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 55.
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=rrnAC2831;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV47585.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY596297; AAV47585.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_049939062.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UYR8; -.
DR   STRING; 272569.rrnAC2831; -.
DR   EnsemblBacteria; AAV47585; AAV47585; rrnAC2831.
DR   GeneID; 40153682; -.
DR   KEGG; hma:rrnAC2831; -.
DR   PATRIC; fig|272569.17.peg.3404; -.
DR   eggNOG; arCOG04076; Archaea.
DR   HOGENOM; CLU_120795_0_0_2; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000001169; Chromosome I.
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..179
FT                   /note="GTP-dependent dephospho-CoA kinase"
FT                   /id="PRO_0000380047"
SQ   SEQUENCE   179 AA;  18872 MW;  6FF60BFBB5BCB1AF CRC64;
     MSDVVLELPS DLRHELKEPL GRIYTDTAAL LADAGDPIIA VGDMVTYHLI EAGRTPDLAL
     VDERTERSAV DADVAAAIDG FDRTLSVDNP AATLTADLLA ALRDGLDSDE TTLLDVDGEE
     DLATLPAVLA APAGASVVYG QPDEGMVLAD CDDTARDRVR SLLERMDGDA ERAIALVSN