ID   CPGS_PYRFU              Reviewed;         431 AA.
AC   Q8U4K6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=PF0079;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL80203.1; -; Genomic_DNA.
DR   RefSeq; WP_011011191.1; NC_003413.1.
DR   AlphaFoldDB; Q8U4K6; -.
DR   STRING; 186497.PF0079; -.
DR   PRIDE; Q8U4K6; -.
DR   EnsemblBacteria; AAL80203; AAL80203; PF0079.
DR   GeneID; 1467908; -.
DR   KEGG; pfu:PF0079; -.
DR   PATRIC; fig|186497.12.peg.83; -.
DR   eggNOG; arCOG01230; Archaea.
DR   HOGENOM; CLU_638764_0_0_2; -.
DR   OMA; RRCGGGM; -.
DR   OrthoDB; 18931at2157; -.
DR   PhylomeDB; Q8U4K6; -.
DR   Proteomes; UP000001013; 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..431
FT                   /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT                   /id="PRO_0000313695"
SQ   SEQUENCE   431 AA;  47393 MW;  7D536F9EFB44F5D1 CRC64;
     MKLALIDGEH YPDVNRWAIE KIKPCCAVFV GGTEKIGSIR DIEKALNIKV YHSPNIFEAL
     SKAISENNIT EVIDLSDEPV LTPNLRFRIA SYLLKLGITY KGADFEFRAK EWKKIDIPSI
     SIIGTGKRVG KTAIGGFVGR TLKELYKVVI VTMGRGGPEK PEVIRGDLME ITPEFLLKVS
     EEGKHAASDH FEDALTAGVI TVGCRRCGGG LAGFSFFDII DEGIEIAKSL NPDIIVFEGS
     GPTFPNVLAD GFITITSAIH GTEKIEQYFG PLRIGLADIV VVTMADSVSE EKLKRITQAI
     REINPEADIH LTRFVPRLIG EVDGKAIIAT TNPQSAKKFS EELEKMGIEV VYYTGNLAKR
     NILKDELAKV NYDDTAIVEL KAGAVDVVIR HAFSRGKRVV FLDNEPKNID GKDLKEAVIN
     LARRIVNDKG N