ID   CPGS_THEKO              Reviewed;         432 AA.
AC   Q5JDW8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=TK1039;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD85228.1; -; Genomic_DNA.
DR   RefSeq; WP_011249990.1; NC_006624.1.
DR   AlphaFoldDB; Q5JDW8; -.
DR   STRING; 69014.TK1039; -.
DR   PRIDE; Q5JDW8; -.
DR   EnsemblBacteria; BAD85228; BAD85228; TK1039.
DR   GeneID; 3234389; -.
DR   KEGG; tko:TK1039; -.
DR   PATRIC; fig|69014.16.peg.1016; -.
DR   eggNOG; arCOG01230; Archaea.
DR   HOGENOM; CLU_638764_0_0_2; -.
DR   OMA; RRCGGGM; -.
DR   OrthoDB; 18931at2157; -.
DR   PhylomeDB; Q5JDW8; -.
DR   Proteomes; UP000000536; 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; Reference proteome.
FT   CHAIN           1..432
FT                   /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT                   /id="PRO_0000313697"
SQ   SEQUENCE   432 AA;  47355 MW;  DD38349C98486D1D CRC64;
     MRVVLIDGEH YPDVTKWAIH KLGDVCCAVF LGGTEKIGSL KALEDKIGVP LYHSPNYLDA
     LKRAVLENDV EEVVDLSDEP VLTYEDRFRI ASLCMLLGVT YRGADFTFTP KPLKKTKKPS
     ISIIGTGKRV GKTAVSGFVA RTLKEVARPV VVTMGRGGPE EPELIEGEKI ELTPQFLLKV
     AKEGKHAASD HFEDALTSRV TTIGCRRCGG GMAGFPFFDV VDKGVELAES LPHDLIILEG
     SGATFPAYRT DAYILIIGGR QKTDFLRGYF GPFRIALADL IIVTMSDEIN PEKRAEIRKI
     VEEINPKADL HFTAFRPRPL GNISGKKLGL VMTSQSALPK AKEHLEGLGA EVVATSGNLS
     NRPKLREDLE KFRGIDAVAV ELKAAAVDVV TKWALERGIE VIYLDNEPVN IDGKDLRKSV
     LELGKRVLGR RA