PGK2_METVS
ID PGK2_METVS Reviewed; 313 AA.
AC A6UQ76;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=2-phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00769};
DE Short=2PGK {ECO:0000255|HAMAP-Rule:MF_00769};
DE EC=2.7.2.16 {ECO:0000255|HAMAP-Rule:MF_00769};
GN Name=pgk2 {ECO:0000255|HAMAP-Rule:MF_00769}; OrderedLocusNames=Mevan_0742;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00769};
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}.
CC -!- SIMILARITY: Belongs to the 2-phosphoglycerate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00769}.
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DR EMBL; CP000742; ABR54648.1; -; Genomic_DNA.
DR RefSeq; WP_011972550.1; NC_009634.1.
DR AlphaFoldDB; A6UQ76; -.
DR STRING; 406327.Mevan_0742; -.
DR PRIDE; A6UQ76; -.
DR EnsemblBacteria; ABR54648; ABR54648; Mevan_0742.
DR GeneID; 5325536; -.
DR KEGG; mvn:Mevan_0742; -.
DR eggNOG; arCOG01967; Archaea.
DR HOGENOM; CLU_848909_0_0_2; -.
DR OMA; EMPFSKG; -.
DR OrthoDB; 57277at2157; -.
DR UniPathway; UPA00551; UER00609.
DR Proteomes; UP000001107; 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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..313
FT /note="2-phosphoglycerate kinase"
FT /id="PRO_1000062237"
FT DOMAIN 8..95
FT /note="ATP-cone"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ SEQUENCE 313 AA; 35903 MW; A9B8DED9797925FA CRC64;
MTFEEITNKI LVKDKDYEMP FSKGLLTRSL TAAGMKPSES YILAREIERD LTDQGLRKIS
KDELRRRVYY ALINRDYEDI AEKYLLWRRV LKKHSIIILV GGASGVGTST IAFELASRLG
IPSVIGTDSI REVMRRSISK DLVPMLYESS YTAWKALRHS SAEEYDTKEM HLLGFERHVE
PVLIGIESII DRSLTEGMSV ILEGTHIVPG LLGEKYHSMQ NVIILNLTLS SEEIHKQRFV
ARAKVSDRPL ERYLSNFEII KEINEYIVKK SRENKVPVIE NVSISETVQK CLEIVTDRFV
DLNEESEADS EIY
