CPGS_PYRHO
ID CPGS_PYRHO Reviewed; 435 AA.
AC O74083; O57881;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=PH0150;
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 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}.
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DR EMBL; BA000001; BAA29219.1; -; Genomic_DNA.
DR PIR; D71236; D71236.
DR AlphaFoldDB; O74083; -.
DR STRING; 70601.3256536; -.
DR EnsemblBacteria; BAA29219; BAA29219; BAA29219.
DR KEGG; pho:PH0150; -.
DR eggNOG; arCOG01230; Archaea.
DR OMA; RRCGGGM; -.
DR Proteomes; UP000000752; 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..435
FT /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT /id="PRO_0000313696"
SQ SEQUENCE 435 AA; 48098 MW; C8DA6015EF9D091D CRC64;
MGYAMRLALI DGEHYPDVNR WALEKLKVDC AVFVGGMEKI GSIRDVERTL SIKLYYDEDI
FKALERAIEE NEIREVIDLS DEPVLTPEIR FRIASFLLKR GITYIGADFE FKPKEWIKID
VPSINIIGTG KRIGKTAIGG FVGRTLKEEY KVVIVTMGRG GPESPEVIRG DLMEITPEFL
VEVSEKGRHA ASDHFEDALT AGVATVGCRR CGGGLAGFTF LDVLQKGIEV AKSLNPEIIV
FEGSGASFAN VLSEGFITVV SALQGKEIKM YLYPLRISLG DLIVVTMADE VKDPGKISSL
IKEINPDADI HLTRFSPRLI GNVEGKAVVV TTSTNSAKRV TKELEDRGID VVGFSGNLAN
RVKLREELKK VSYDTLIVEL KAGAVDVAIK SALRSGKRIV FLDYEPKNID DKDLRESVKE
LARRIVNDKG HRKGR
