PGK2_METM5
ID PGK2_METM5 Reviewed; 313 AA.
AC A4FW93;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=MmarC5_0147;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-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; CP000609; ABO34464.1; -; Genomic_DNA.
DR RefSeq; WP_011867924.1; NC_009135.1.
DR AlphaFoldDB; A4FW93; -.
DR STRING; 402880.MmarC5_0147; -.
DR EnsemblBacteria; ABO34464; ABO34464; MmarC5_0147.
DR GeneID; 4927834; -.
DR KEGG; mmq:MmarC5_0147; -.
DR eggNOG; arCOG01967; Archaea.
DR HOGENOM; CLU_848909_0_0_2; -.
DR OMA; EMPFSKG; -.
DR OrthoDB; 57277at2157; -.
DR UniPathway; UPA00551; UER00609.
DR Proteomes; UP000000253; 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_1000062235"
FT DOMAIN 8..95
FT /note="ATP-cone"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ SEQUENCE 313 AA; 35988 MW; 54142BE30FF6C6C4 CRC64;
MTFDENISRI LVKDKEYEMP FSKGLLARSL TAAGMKPSES YTLAREIERD LNEQNVLKIS
KDELRRRVYY TLINRDYEGI GEKYLLWRRV LKKHSIIILV GGSSGVGTST IAFELASRLG
IPSVIGTDSI REVMRRSISK DLVPMLYESS YTAWTALRRS QWDEQDTKEM HLLGFERHVE
PVLLGIESII DRSLTEGTSV IIEGTHIVPG LMGEKYQSMP NVIFLNLTLS SEETHKKRFT
ARAKVSDRPL ERYLENFEII KEINQYIVEK SKENKVPVIE NVSISETVQK CLEIVTERFS
NLNDEPIIDS DMY
