PGK2_METM7
ID PGK2_METM7 Reviewed; 312 AA.
AC A6VH17;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=MmarC7_0676;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
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; CP000745; ABR65743.1; -; Genomic_DNA.
DR RefSeq; WP_011977065.1; NC_009637.1.
DR AlphaFoldDB; A6VH17; -.
DR STRING; 426368.MmarC7_0676; -.
DR PRIDE; A6VH17; -.
DR EnsemblBacteria; ABR65743; ABR65743; MmarC7_0676.
DR GeneID; 5328682; -.
DR KEGG; mmz:MmarC7_0676; -.
DR eggNOG; arCOG01967; Archaea.
DR HOGENOM; CLU_848909_0_0_2; -.
DR OMA; EMPFSKG; -.
DR OrthoDB; 57277at2157; -.
DR UniPathway; UPA00551; UER00609.
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..312
FT /note="2-phosphoglycerate kinase"
FT /id="PRO_1000062236"
FT DOMAIN 8..95
FT /note="ATP-cone"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ SEQUENCE 312 AA; 35750 MW; 82510EF90BC119BF CRC64;
MTFDENISRI LVTDKEYDMP FSKGLLARSL SAAGMKPSES YTLAREIERD LTEQNVLKIS
KDELRRRVYY TLINRDYEGI GEKYLLWRRV LKKHSIIILV GGSSGVGTST IAFELASRLG
IPSVIGTDSI REVMRRSISK DLVPMLYESS YTAWTALRRS QWEEQDTKGM HLLGFERHVE
PVLLGIESII DRSLTEGTSV IIEGTHIVPG LMGEKYQSMP NVIFLNLTLS SEEIHKKRFT
ARAKVSDRPL ERYLENFEII KEINQYIVEK SKENNVPVIE NVSISETVQK CLEIVTERFS
NLTDEPIDSD FY
