ID   CPGS_METS3              Reviewed;         458 AA.
AC   A5UJB8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=Msm_0091;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(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; CP000678; ABQ86296.1; -; Genomic_DNA.
DR   RefSeq; WP_004034011.1; NC_009515.1.
DR   AlphaFoldDB; A5UJB8; -.
DR   STRING; 420247.Msm_0091; -.
DR   EnsemblBacteria; ABQ86296; ABQ86296; Msm_0091.
DR   GeneID; 5215753; -.
DR   KEGG; msi:Msm_0091; -.
DR   PATRIC; fig|420247.28.peg.94; -.
DR   eggNOG; arCOG01230; Archaea.
DR   HOGENOM; CLU_638764_0_0_2; -.
DR   OMA; RRCGGGM; -.
DR   Proteomes; UP000001992; 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..458
FT                   /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT                   /id="PRO_0000313690"
SQ   SEQUENCE   458 AA;  50966 MW;  061D6A3045A5530B CRC64;
     MKSISKMLCL VDGEHYLPVT QESIDVLNNL EHIDIVAAVF IGGTEKLRDD SEESYSKVLG
     VPVQFAKNED IPYDIIVEMI NRYDVDTVMD LSDEPILDYP KRFKIACKTL AQGVSYQGPD
     FKFDPVTQYE IMEKPSIKII GTGKRIGKTA VSGFVSRLID KNGYEPCVIA MGRGGPQEPE
     IVHGEQLEIT PEFLLEQSEK GVHAASDHWE DALMSRILTI GCRRCGGGMA GEVFLTNMKK
     GAKLANQVDS KFAIFEGSGA AIPPIKTNKN IVLIGANQPL NNIIDYFGPY RIGLGDLIIL
     TMCEEPMCNE EKREYIEKFI KEINPKAKII STVFRPKPLA DISGKKVLFA TTAPKSIEHE
     LVDYLETNYN CEIVGTTPHL SNRPLLKKDI EKYMDEADIM LTELKAAAVD VATKDSIKAG
     LDVVYCDNIP VPINYKYPDL SKSVLEIVDE AIEDFNKD