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