ID   PGK2_METMP              Reviewed;         312 AA.
AC   Q6LXC1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=MMP1431;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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, ECO:0000305}.
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DR   EMBL; BX950229; CAF30987.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6LXC1; -.
DR   STRING; 267377.MMP1431; -.
DR   EnsemblBacteria; CAF30987; CAF30987; MMP1431.
DR   KEGG; mmp:MMP1431; -.
DR   PATRIC; fig|267377.15.peg.1467; -.
DR   eggNOG; arCOG01967; Archaea.
DR   HOGENOM; CLU_848909_0_0_2; -.
DR   OMA; EMPFSKG; -.
DR   BioCyc; MMAR267377:MMP_RS07365-MON; -.
DR   UniPathway; UPA00551; UER00609.
DR   Proteomes; UP000000590; 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; Reference proteome; Transferase.
FT   CHAIN           1..312
FT                   /note="2-phosphoglycerate kinase"
FT                   /id="PRO_0000156150"
FT   DOMAIN          7..94
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ   SEQUENCE   312 AA;  35858 MW;  E6D92B57C75D05A5 CRC64;
     MTFDDNIRIL VKDKEYDMPF SKGLLARSLT AAGMKPSASY TLARDIEREL NEQNVLKISK
     DELRRRVYYT LINRDYEAIA EKYLLWRRIL KKHSIIILVG GSSGVGTSTI AFELASRLGI
     PSVIGTDSIR EVMRRSISKD LVPMLYESSY TAWTALRKSS WEEQDSKEMH LLGFERHVEP
     VLLGIESIID RSLTEGTSVI IEGTHIVPGL MAEKYQEMPN VIFLNLTLSS EETHKKRFIA
     RAKVSDRPLE RYLENFEIIK EINQYIVEKS KENNLPVIEN VSISDTVQKC LEIVTERFSN
     LNDEPIIDSD FY