ID   PGK2_METTH              Reviewed;         306 AA.
AC   O27911;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=MTH_1883;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000666; AAB86349.1; -; Genomic_DNA.
DR   PIR; A69119; A69119.
DR   RefSeq; WP_010877485.1; NC_000916.1.
DR   AlphaFoldDB; O27911; -.
DR   STRING; 187420.MTH_1883; -.
DR   EnsemblBacteria; AAB86349; AAB86349; MTH_1883.
DR   GeneID; 1470968; -.
DR   KEGG; mth:MTH_1883; -.
DR   PATRIC; fig|187420.15.peg.1838; -.
DR   HOGENOM; CLU_848909_0_0_2; -.
DR   OMA; EMPFSKG; -.
DR   UniPathway; UPA00551; UER00609.
DR   Proteomes; UP000005223; 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..306
FT                   /note="2-phosphoglycerate kinase"
FT                   /id="PRO_0000156148"
FT   DOMAIN          1..90
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ   SEQUENCE   306 AA;  34884 MW;  3B3457B05908AC76 CRC64;
     MIMVQGEVSG KKYTEPFSKG VLARSLTRAE MDPNRAYTFA SRIEAHLKKN KVDLITIEEL
     VEIVSEHLRK EDPEVAEKYM LWRKIRQCKE PLIILIGGAS GVGTSSIAFE VANRLGIRNM
     ISTDMIREVM RKIVSRELLP SIYESSYTAY QSLRIPPPPE LDEVLIGFRD HVESVSIGVE
     AVIERALTEG ISIVIEGVHI VPGFIREDLV NKENVAMFVL TVSDENVHKG RFYSRCRQMW
     ARRPLKRYIS YFWAIRRIHR YIENQARKHG VPVIENIDVV TTIDSIIKSL TKTTVKGGEK
     GAEKTE