ID   CPGS_METTH              Reviewed;         464 AA.
AC   O26325;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Cyclic 2,3-diphosphoglycerate synthetase;
DE            Short=cDPGS;
DE            EC=6.5.1.9 {ECO:0000269|Ref.2};
GN   Name=cpgS; OrderedLocusNames=MTH_223;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, INDUCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   DOI=10.1007/BF00314474;
RA   van Alebeek G.-J.W.M., Tafazzul G., Kreuwels M.J.J., Keltjens J.T.,
RA   Vogels G.D.;
RT   "Cyclic 2,3-diphosphoglycerate metabolism in Methanobacterium
RT   thermoautotrophicum (strain Delta H): characterization of the synthetase
RT   reaction.";
RL   Arch. Microbiol. 162:193-198(1994).
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. Not able to catalyze cDPG hydrolysis. May be involved
CC       in osmotic balance. {ECO:0000269|Ref.2}.
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:0000269|Ref.2};
CC   -!- ACTIVITY REGULATION: Activity decreases in response to phosphate
CC       limitation. {ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.0 mM for ATP {ECO:0000269|Ref.2};
CC         KM=21 mM for 2,3 diphosphoglycerate {ECO:0000269|Ref.2};
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 65 degrees Celsius. {ECO:0000269|Ref.2};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.2}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the cyclic 2,3-diphosphoglycerate synthetase
CC       family. {ECO:0000305}.
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DR   EMBL; AE000666; AAB84729.1; -; Genomic_DNA.
DR   PIR; F69127; F69127.
DR   AlphaFoldDB; O26325; -.
DR   STRING; 187420.MTH_223; -.
DR   EnsemblBacteria; AAB84729; AAB84729; MTH_223.
DR   KEGG; mth:MTH_223; -.
DR   PATRIC; fig|187420.15.peg.192; -.
DR   HOGENOM; CLU_638764_0_0_2; -.
DR   OMA; RRCGGGM; -.
DR   Proteomes; UP000005223; 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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..464
FT                   /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT                   /id="PRO_0000313689"
SQ   SEQUENCE   464 AA;  51320 MW;  0E73237125CE399F CRC64;
     MFMKATETMI CLVDGEHYLP VTRAAVETLD SMEHIDVKAL IFIGGTEKLR TSSPEEYTEI
     MGRPVHFGDD PHRIPYKLIG ELIRKYGADT VMDLSDEPVL DYSKRFRIAS VVLGEGAVYR
     GPDFEFQPLT EYDILEKPSL KILGTGKRIG KTAVSAYAAR LIHERQYNPC VVAMGRGGPE
     EPEIVHGDRI EITPEFLMEQ SDKGVHAASD HWEDALMSRI LTVGCRRCGG GMVGDVFITN
     MKRGAETANR LDADFVILEG SGAAIPPVKS NRHIVLVGAN QPLINIKNFF GPFRIGLADL
     VIVTMCEEPM AGDEKVREIV DFIESINPEA EVITTVFRPK PLGEIEGKNV LFATTAPDSV
     KDLLVEYLES EYSCRVVGTT PHLSNRPLLQ RDIERYIEDA DVMLTELKAA AVDVATKDAL
     EAGLEVIYCD NIPVVRDGAQ DELDDAIISV VERAIADFNL RKTP