PGK2_METFV
ID PGK2_METFV Reviewed; 304 AA.
AC Q49156; E3GXL8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=2-phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00769, ECO:0000303|PubMed:2226838};
DE Short=2PGK {ECO:0000255|HAMAP-Rule:MF_00769, ECO:0000303|PubMed:2226838};
DE EC=2.7.2.16 {ECO:0000255|HAMAP-Rule:MF_00769, ECO:0000269|PubMed:2226838, ECO:0000269|PubMed:8159166};
GN Name=pgk2 {ECO:0000255|HAMAP-Rule:MF_00769}; OrderedLocusNames=Mfer_0247;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND PATHWAY.
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX PubMed=8159166; DOI=10.1007/bf00391009;
RA Lehmacher A., Hensel R.;
RT "Cloning, sequencing and expression of the gene encoding the 2-
RT phosphoglycerate kinase from Methanothermus fervidus.";
RL Mol. Gen. Genet. 242:163-168(1994).
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, COFACTOR, AND PATHWAY.
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 phosphorylation of 2-phosphoglycerate to 2,3-
CC diphosphoglycerate. Involved in the biosynthesis of cyclic 2,3-
CC bisphosphoglycerate, a thermoprotectant. {ECO:0000255|HAMAP-
CC Rule:MF_00769, ECO:0000269|PubMed:2226838, ECO:0000269|PubMed:8159166}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate + ATP = (2R)-2,3-bisphosphoglycerate +
CC ADP + H(+); Xref=Rhea:RHEA:42408, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58248, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:456216; EC=2.7.2.16; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00769, ECO:0000269|PubMed:2226838,
CC ECO:0000269|PubMed:8159166};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00769,
CC ECO:0000269|PubMed:2226838, ECO:0000269|PubMed:8159166};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for 2-phosphoglycerate {ECO:0000269|PubMed:8159166};
CC KM=2.7 mM for ATP {ECO:0000269|PubMed:8159166};
CC -!- PATHWAY: Thermoadapter biosynthesis; cyclic 2,3-diphosphoglycerate
CC biosynthesis; cyclic 2,3-diphosphoglycerate from 2-phospho-D-glycerate:
CC step 1/2. {ECO:0000255|HAMAP-Rule:MF_00769, ECO:0000305|PubMed:2226838,
CC ECO:0000305|PubMed:8159166}.
CC -!- SIMILARITY: Belongs to the 2-phosphoglycerate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00769, ECO:0000305}.
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DR EMBL; X70785; CAA50058.1; -; Genomic_DNA.
DR EMBL; CP002278; ADP77050.1; -; Genomic_DNA.
DR PIR; S41582; S41582.
DR RefSeq; WP_013413328.1; NC_014658.1.
DR AlphaFoldDB; Q49156; -.
DR STRING; 523846.Mfer_0247; -.
DR EnsemblBacteria; ADP77050; ADP77050; Mfer_0247.
DR GeneID; 9961962; -.
DR KEGG; mfv:Mfer_0247; -.
DR HOGENOM; CLU_848909_0_0_2; -.
DR OMA; EMPFSKG; -.
DR OrthoDB; 57277at2157; -.
DR BioCyc; MetaCyc:MON-20995; -.
DR BRENDA; 2.7.2.16; 3286.
DR SABIO-RK; Q49156; -.
DR UniPathway; UPA00551; UER00609.
DR Proteomes; UP000002315; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00769; 2PGK; 1.
DR InterPro; IPR020872; 2PKG.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF03477; ATP-cone; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..304
FT /note="2-phosphoglycerate kinase"
FT /id="PRO_0000156152"
FT DOMAIN 2..90
FT /note="ATP-cone"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ SEQUENCE 304 AA; 35036 MW; 3CEBCF552B51C954 CRC64;
MILVEGKVAG KKYREPFSKG VLARSLTRSG MDPTDAYLLA AEVESYLKKE KKKIVTIDEL
VKIVYNKLKE KDEKIAEKYI RWRKIREYKE PLILLIAGAS GVGTSSIAFE VANRLGIRNM
ISTDMIREVM RKMISKELIP SLHESTFTAY KSLRTPAPVE FDEVLVGFRD HVNVVTVGIE
AVIERALTEG ISIVIEGAHL VPGFIREELI NKNNVAMFVL TVPDEKMHRS RFYSRCRQKW
ARRPLERYLK YFWAIRRIHD YIEMQARKHN IPIIENIDVV TTIDSIVKSL TEDLVHKDVG
KYKG
