ID   CPGS_THESM              Reviewed;         434 AA.
AC   C6A0T3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
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=TSIB_0160;
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739;
RX   PubMed=19447963; DOI=10.1128/aem.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
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; CP001463; ACS89228.1; -; Genomic_DNA.
DR   RefSeq; WP_012766189.1; NC_012883.1.
DR   AlphaFoldDB; C6A0T3; -.
DR   STRING; 604354.TSIB_0160; -.
DR   EnsemblBacteria; ACS89228; ACS89228; TSIB_0160.
DR   GeneID; 8095132; -.
DR   KEGG; tsi:TSIB_0160; -.
DR   eggNOG; arCOG01230; Archaea.
DR   HOGENOM; CLU_638764_0_0_2; -.
DR   OMA; RRCGGGM; -.
DR   OrthoDB; 18931at2157; -.
DR   Proteomes; UP000009079; 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.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..434
FT                   /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT                   /id="PRO_1000216179"
SQ   SEQUENCE   434 AA;  47998 MW;  DD99DB334D50CD0C CRC64;
     MRMVLIDGEH YPDVTAWAIK KIGDVSCAVF LGGTEKIGDM KSLEEKIGVK LYYGESYISN
     IKKAINENKI GEVIDLSDEP VLNYEDRFRI AAVLLKHGIK YKGADFEFSP KEMVQINKPS
     LTILGTGKRV GKTAISGFVA RTLKEISKPI IVTMGRGGPE EPEIIEGNKL EITPDFLVRV
     AESGKHAASD HFEDALTSRV ITIGCRRCGG GMVGFSFFDI VNKGIKLAEK LEGDIVILEG
     SGATFPAVKA DKYITVVGAT QRIEFIKSYF GPFRIGLADL IVITLADMVS KEKIEKIQKI
     IESINPDAEI HLTAFKPRPL SEIKGKKAIL VMTAPPEGLE KAARHLENRY DVEIVGKSAN
     LANRPKLIED LSRFKYYDTV LVELKAAAVD VATKEALKYG KEVIYIDNEP VNIDNKNLRE
     AVLEIGWELK GERK