ID   CPGS_METKA              Reviewed;         456 AA.
AC   Q8TY02;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=MK0505;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM01720.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TY02; -.
DR   STRING; 190192.MK0505; -.
DR   EnsemblBacteria; AAM01720; AAM01720; MK0505.
DR   KEGG; mka:MK0505; -.
DR   PATRIC; fig|190192.8.peg.536; -.
DR   HOGENOM; CLU_638764_0_0_2; -.
DR   OMA; RRCGGGM; -.
DR   Proteomes; UP000001826; 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   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..456
FT                   /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT                   /id="PRO_0000313691"
SQ   SEQUENCE   456 AA;  49620 MW;  0957551F80576226 CRC64;
     MTAVKRILAL VDGEHYIPVT REALETVEEL DLGELVGAVF IGGTEKISEP EAVKRELGVR
     VWLSESEDEI PVDMIVKVIE EEDVDVVLDL SDEPVVSPDN RFEIASAVLS AGAEYWCPDL
     RLKPVEFHDV LEKPSLRIIG TGKRVGKTAV SAYTCRVLNA RGYNPCVVVM GRGGPREPEI
     VRGDEIELTP EYLLKEAEKG KHAASDHWED ALLSRIPTVG CRRCAGGLAG RTFTTNIVRG
     AKIANELPAD FVVVEGSGAA VPPIKTDAGI VIVGANQPLE HIGGYLGPYR IRMCDLAIIT
     MCEEPMADDA KIRKVERTVR EAGDGIEVVL SVFRPKPTED VEGKRAMFVT TAPEEVVSRL
     VEHLEEEYGC EIVGTSPHLS NRPKLRKDLE KYIDDADILL TELKAAAVDV ATREALKAGL
     GVVYVDNVPI AVGGDYDHVG DAVENVAELA IDRFEG