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DPCKG_PYRAB
ID   DPCKG_PYRAB             Reviewed;         179 AA.
AC   Q9UY21; G8ZK48;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=PYRAB16870; ORFNames=PAB1106;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248288; CAB50591.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE71155.1; -; Genomic_DNA.
DR   PIR; A75019; A75019.
DR   RefSeq; WP_010868805.1; NC_000868.1.
DR   AlphaFoldDB; Q9UY21; -.
DR   STRING; 272844.PAB1106; -.
DR   EnsemblBacteria; CAB50591; CAB50591; PAB1106.
DR   GeneID; 1495984; -.
DR   KEGG; pab:PAB1106; -.
DR   PATRIC; fig|272844.11.peg.1801; -.
DR   eggNOG; arCOG04076; Archaea.
DR   HOGENOM; CLU_120795_1_0_2; -.
DR   OMA; AIYDHKT; -.
DR   OrthoDB; 116732at2157; -.
DR   PhylomeDB; Q9UY21; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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_0000137613"
SQ   SEQUENCE   179 AA;  19929 MW;  E5A0E1088B591A32 CRC64;
     MKVLFKLPPS LRSELKKPVG ELIEGDIPTP YLKVKDILTN EDPLVTVGDV VTENIMKVGL
     NPNLAIYDHK TERREYKPNI RSVEGVLITV KNPPGTITLP LLKAIKKAYS LLSHGKRVHI
     VVDGEEDLAT IPAVLYAPIG TTVIYGQPKK GIVLIKVTNE CKRRCAKIMR RMEVVRNGD
 
 
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