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CPGS_PYRAB
ID   CPGS_PYRAB              Reviewed;         427 AA.
AC   Q9V2C5; G8ZFY4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Cyclic 2,3-diphosphoglycerate synthetase {ECO:0000255|HAMAP-Rule:MF_01908};
DE            Short=cDPGS {ECO:0000255|HAMAP-Rule:MF_01908};
DE            EC=6.5.1.9 {ECO:0000255|HAMAP-Rule:MF_01908};
GN   Name=cpgS {ECO:0000255|HAMAP-Rule:MF_01908}; OrderedLocusNames=PYRAB01490;
GN   ORFNames=PAB2252;
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 formation of cyclic 2,3-diphosphoglycerate
CC       (cDPG) by formation of an intramolecular phosphoanhydride bond at the
CC       expense of ATP. {ECO:0000255|HAMAP-Rule:MF_01908}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-bisphosphoglycerate + ATP + H(+) = ADP + cyclic (2R)-
CC         2,3-bisphosphoglycerate + phosphate; Xref=Rhea:RHEA:42412,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58248, ChEBI:CHEBI:79081, ChEBI:CHEBI:456216; EC=6.5.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01908};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01908}.
CC   -!- SIMILARITY: Belongs to the cyclic 2,3-diphosphoglycerate synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01908}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB49073.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ248283; CAB49073.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE69525.1; -; Genomic_DNA.
DR   PIR; B75203; B75203.
DR   RefSeq; WP_048146493.1; NC_000868.1.
DR   AlphaFoldDB; Q9V2C5; -.
DR   STRING; 272844.PAB2252; -.
DR   EnsemblBacteria; CAB49073; CAB49073; PAB2252.
DR   GeneID; 1495036; -.
DR   KEGG; pab:PAB2252; -.
DR   PATRIC; fig|272844.11.peg.162; -.
DR   eggNOG; arCOG01230; Archaea.
DR   HOGENOM; CLU_638764_0_0_2; -.
DR   OrthoDB; 18931at2157; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0036356; F:cyclic 2,3-diphosphoglycerate synthetase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01908; Cyc_PG_syn; 1.
DR   InterPro; IPR016557; Cyc_diphosphoglycerate_synth.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PIRSF; PIRSF009445; Cyc_PG_syn; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..427
FT                   /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT                   /id="PRO_0000313694"
SQ   SEQUENCE   427 AA;  47153 MW;  56A969B00BBA3F1D CRC64;
     MRIALIDGEH YPDVNRWALE KLNVECAVFI GGMEKIGSIE DVERALNVKL YHDKDPFKAL
     EKALEENDVE EVIDLSDEPV MTPELRFRIA SYLLKRGIAY KGADFEFRPK EWIKLEVPSI
     NIIGTGKRVG KTAIGGFVGR TLKERYRIVI VTMGRGGPEK PEIIRGDKIT ITPEFLVKIA
     EQGRHAASDH FEDALTAGVP TIGCRRCGGG LAGFTFLDVV KEGIEVAKTL KPELIVLEGS
     GASFANVLSD GFITVVSALQ GERIKTYMYP LRISLADIVV VTMVEEVSEG EKIKRIIKEI
     NPDADVHLTR FAPRLIGNVE GKAIVLTTSQ ESAKKMAKEL ERKGIEIAGY SGNLANRGRL
     REEMNRFNYD TVIVELKAGA VDVAIREALS NGKKVVFLDN EPVNVDGKNL KSAIKKLAER
     ILHDKGG
 
 
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