CPGS_METFV
ID CPGS_METFV Reviewed; 460 AA.
AC O93732; E3GWZ2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Cyclic 2,3-diphosphoglycerate synthetase;
DE Short=cDPGS;
DE EC=6.5.1.9 {ECO:0000269|PubMed:2226838};
GN Name=cpgS; OrderedLocusNames=Mfer_0077;
OS Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanothermaceae; Methanothermus.
OX NCBI_TaxID=523846;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX PubMed=9811660; DOI=10.1128/jb.180.22.5997-6004.1998;
RA Matussek K., Moritz P., Brunner N., Eckerskorn C., Hensel R.;
RT "Cloning, sequencing, and expression of the gene encoding cyclic 2,3-
RT diphosphoglycerate synthetase, the key enzyme of cyclic 2,3-
RT diphosphoglycerate metabolism in Methanothermus fervidus.";
RL J. Bacteriol. 180:5997-6004(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX PubMed=21304736; DOI=10.4056/sigs.1283367;
RA Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL Stand. Genomic Sci. 3:315-324(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX PubMed=2226838; DOI=10.1016/0014-5793(90)80456-s;
RA Lehmacher A., Vogt A.-B., Hensel R.;
RT "Biosynthesis of cyclic 2,3-diphosphoglycerate. Isolation and
RT characterization of 2-phosphoglycerate kinase and cyclic 2,3-
RT diphosphoglycerate synthetase from Methanothermus fervidus.";
RL FEBS Lett. 272:94-98(1990).
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. It is also able to catalyze the hydrolysis of cDPG but
CC with significant slower rates (8-10 times). May be involved in
CC thermoadaptation. {ECO:0000269|PubMed:2226838,
CC ECO:0000269|PubMed:9811660}.
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|PubMed:2226838};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 mM for ATP (at pH 7.0 and 83 degrees Celsius)
CC {ECO:0000269|PubMed:2226838, ECO:0000269|PubMed:9811660};
CC KM=5.8 mM for 2,3 diphosphoglycerate (at pH 7.0 and 83 degrees
CC Celsius) {ECO:0000269|PubMed:2226838, ECO:0000269|PubMed:9811660};
CC KM=4.7 mM for ADP (at pH 7.0 and 83 degrees Celsius)
CC {ECO:0000269|PubMed:2226838, ECO:0000269|PubMed:9811660};
CC KM=41.2 mM for cyclic 2,3-diphosphoglycerate (at pH 7.0 and 83
CC degrees Celsius) {ECO:0000269|PubMed:2226838,
CC ECO:0000269|PubMed:9811660};
CC Vmax=32 umol/min/mg enzyme for cDPG synthesis (at pH 7.0 and 83
CC degrees Celsius) {ECO:0000269|PubMed:2226838,
CC ECO:0000269|PubMed:9811660};
CC Vmax=4 umol/min/mg enzyme for cDPG hydrolysis (at pH 7.0 and 83
CC degrees Celsius) {ECO:0000269|PubMed:2226838,
CC ECO:0000269|PubMed:9811660};
CC pH dependence:
CC Optimum pH is 5.0-7.5. {ECO:0000269|PubMed:2226838,
CC ECO:0000269|PubMed:9811660};
CC Temperature dependence:
CC Optimum temperature is 75-80 degrees Celsius.
CC {ECO:0000269|PubMed:2226838, ECO:0000269|PubMed:9811660};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:9811660}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=50663; Mass_error=6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9811660};
CC -!- SIMILARITY: Belongs to the cyclic 2,3-diphosphoglycerate synthetase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y09856; CAA70986.1; -; Genomic_DNA.
DR EMBL; CP002278; ADP76881.1; -; Genomic_DNA.
DR RefSeq; WP_013413159.1; NC_014658.1.
DR AlphaFoldDB; O93732; -.
DR EnsemblBacteria; ADP76881; ADP76881; Mfer_0077.
DR GeneID; 9961785; -.
DR KEGG; mfv:Mfer_0077; -.
DR HOGENOM; CLU_638764_0_0_2; -.
DR OMA; RRCGGGM; -.
DR OrthoDB; 18931at2157; -.
DR BioCyc; MetaCyc:MON-20994; -.
DR BRENDA; 6.5.1.9; 3286.
DR SABIO-RK; O93732; -.
DR Proteomes; UP000002315; 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; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9811660"
FT CHAIN 2..460
FT /note="Cyclic 2,3-diphosphoglycerate synthetase"
FT /id="PRO_0000313693"
SQ SEQUENCE 460 AA; 50788 MW; A671E3011CB1FE4D CRC64;
MGETKKMICL VDGEHYFPVV KDSIEILDDL EHIDVVAVVF IGGTEKLQIE DPKEYSEKLG
KPVFFGPDPK KIPYDVIKKC VKKYNADIVM DLSDEPVVDY TKRFRIASIV LKEGAVYQGA
DFKFEPLTEY DVLEKPSIKI IGTGKRIGKT AVSAYAARVI HKHKYNPCVV AMGRGGPREP
EIVEGNKIEI TAEYLLEQAD KGVHAASDHW EDALMSRILT VGCRRCGGGM LGDTFITNVK
RGAEIANKLD SDFVIMEGSG AAIPPVKTNR QIVTVGANQP MININNFFGP FRIGLADLVI
ITMCEEPMAT TEKIKKVEKF IKEINPSANV IPTVFRPKPV GNVEGKKVLF ATTAPKVVVG
KLVNYLESKY GCDVVGVTPH LSNRPLLRRD LKKYINKADL MLTELKAAAV DVATRVAIEA
GLDVVYCDNI PVVIDESYGN IDDAIIEVVE MAIDDFKNNR
