ID   PGK2_METM6              Reviewed;         313 AA.
AC   A9A9N2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=MmarC6_1242;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
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., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-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; CP000867; ABX02055.1; -; Genomic_DNA.
DR   RefSeq; WP_012193993.1; NC_009975.1.
DR   AlphaFoldDB; A9A9N2; -.
DR   STRING; 444158.MmarC6_1242; -.
DR   EnsemblBacteria; ABX02055; ABX02055; MmarC6_1242.
DR   GeneID; 5737868; -.
DR   KEGG; mmx:MmarC6_1242; -.
DR   eggNOG; arCOG01967; Archaea.
DR   HOGENOM; CLU_848909_0_0_2; -.
DR   OMA; EMPFSKG; -.
DR   OrthoDB; 57277at2157; -.
DR   PhylomeDB; A9A9N2; -.
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..313
FT                   /note="2-phosphoglycerate kinase"
FT                   /id="PRO_1000200697"
FT   DOMAIN          8..95
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ   SEQUENCE   313 AA;  35879 MW;  66DDD2CE5379218A CRC64;
     MTFDENISRI LVTDKEYDMP FSKGLLARSL SAAGMKPSES YTLAREIERD LNEQNVLKIS
     KDELRRRVYY TLINRDYEGI GEKYLLWRRV LKKHSIIILV GGSSGVGTST IAFELASRLG
     IPSVIGTDSI REVMRRSISK DLVPMLYESS YTAWTALRRS PWDEQDTKEM HLLGFERHVE
     PVLLGIESII DRSLTEGTSV ILEGTHIVPG LMGEKYHSMP NVIFLNLTLS SEETHKKRFT
     ARAKVSDRPL ERYLENFEII KEINQYIVEK SKENNVPVIE NVSISETVQK CLEIVTERFS
     NLNDEPIIDS DIY