ID   CPGS_THEGJ              Reviewed;         438 AA.
AC   C5A4R5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=TGAM_0725;
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS33227.1; -; Genomic_DNA.
DR   RefSeq; WP_015858345.1; NC_012804.1.
DR   AlphaFoldDB; C5A4R5; -.
DR   STRING; 593117.TGAM_0725; -.
DR   PaxDb; C5A4R5; -.
DR   EnsemblBacteria; ACS33227; ACS33227; TGAM_0725.
DR   GeneID; 7987699; -.
DR   KEGG; tga:TGAM_0725; -.
DR   PATRIC; fig|593117.10.peg.725; -.
DR   eggNOG; arCOG01230; Archaea.
DR   HOGENOM; CLU_638764_0_0_2; -.
DR   OMA; RRCGGGM; -.
DR   OrthoDB; 18931at2157; -.
DR   Proteomes; UP000001488; 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   HAMAP; MF_01908; Cyc_PG_syn; 1.
DR   InterPro; IPR016557; Cyc_diphosphoglycerate_synth.
DR   PIRSF; PIRSF009445; Cyc_PG_syn; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..438
FT                   /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT                   /id="PRO_1000216178"
SQ   SEQUENCE   438 AA;  47622 MW;  B483A2657283FEF5 CRC64;
     MKIALIDGEH YPDVVKWALD KLGNVCCAVF LGGSEKIGSL EEVERRLGVP IYRHDDYLTA
     LARALAENPG VKEVVDLSDE PIVGYEDRFR IASLCLLHGV TYRGADFVFK PRPLNRTSKP
     SIGVIGTGKR VGKTAVSGFV ARTLKAITRP VIVTMGRGGP EEPELIDGEK LEITPEFLLR
     IAESGRHAAS DHFEDALTSR VTTIGCRRCG GGMAGFPFFD AVDRGISLAE SLPHDLIILE
     GSGATFPPYR ADAYVVVVGA RQELSSIANY FGPFRLSLAD LVVVTMADLV KEEKIEKIVG
     VVEGVIPRAE VHVTVFRPRP LGDVSGKRIG LVMTSEEALE SSARHLEALG AEVLHSSGNL
     SRRKALLRDL EGFSGIEGIA VELKAAAVDV VTRWALERGI EVIYLDNEPV NIDGKNLREA
     VLRLGKKVLG RRADDTRR