ID   CPGS_THEON              Reviewed;         432 AA.
AC   B6YVF3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=TON_0743;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
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; CP000855; ACJ16231.1; -; Genomic_DNA.
DR   RefSeq; WP_012571703.1; NC_011529.1.
DR   AlphaFoldDB; B6YVF3; -.
DR   STRING; 523850.TON_0743; -.
DR   PRIDE; B6YVF3; -.
DR   EnsemblBacteria; ACJ16231; ACJ16231; TON_0743.
DR   GeneID; 7017045; -.
DR   KEGG; ton:TON_0743; -.
DR   PATRIC; fig|523850.10.peg.746; -.
DR   eggNOG; arCOG01230; Archaea.
DR   HOGENOM; CLU_638764_0_0_2; -.
DR   OMA; RRCGGGM; -.
DR   OrthoDB; 18931at2157; -.
DR   Proteomes; UP000002727; 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..432
FT                   /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT                   /id="PRO_1000188786"
SQ   SEQUENCE   432 AA;  47469 MW;  2F1AD583853CEF34 CRC64;
     MKLVLIDGEH YPDVISWAIK KLGDVCCAVF LGGSEKIGSI GEVERKIGVK VYHSPNYLDA
     LRRALEENKV DEVVDLSDEP VLNYEDRFRI ASLCMLYGVS YRGADFHFKP KPLKKTKKPS
     LAVIGTGKRV GKTAVSGFIA RTLKEIAKPV IVTMGRGGPE EPELIEGDKF EITPEFLLKF
     AESGKHAASD HFEDALTSRV TTIGCRRCGG GMAGFPFFDV VDEGVKLAEN LPNDLIILEG
     SGATFPPYRA DRYVVVVGAK QKLDFVRGYF GTFRVSLADI VVVTMADSVG EERWKALRDA
     ILEINPDVDL HFIAFRPRPL GNVSDKRLGL VMTSSEALPK AKKHLEGLGA EVPYTSDNLS
     KRPLLWRDLE GFRGIDAVAV ELKAAAVDVV TRWALEQGIE VIYLDNEPVN IDGKDLRKAV
     LELGRALLGG RA