ID   PGK_METBR               Reviewed;         409 AA.
AC   P20972;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
DE   Flags: Fragment;
GN   Name=pgk;
OS   Methanobacterium bryantii.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX   NCBI_TaxID=2161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2401408; DOI=10.1016/0378-1119(90)90157-m;
RA   Fabry S., Heppner P., Dietmaier W., Hensel R.;
RT   "Cloning and sequencing the gene encoding 3-phosphoglycerate kinase from
RT   mesophilic Methanobacterium bryantii and thermophilic Methanothermus
RT   fervidus.";
RL   Gene 91:19-25(1990).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; M55530; AAA72937.1; -; Genomic_DNA.
DR   PIR; PN0007; PN0007.
DR   AlphaFoldDB; P20972; -.
DR   SMR; P20972; -.
DR   UniPathway; UPA00109; UER00185.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; -; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PTHR11406; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..>409
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000146056"
FT   BINDING         23..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         359..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         409
SQ   SEQUENCE   409 AA;  44793 MW;  15C13298D649DCE4 CRC64;
     MSLPFYTIDD FNLEDKTVLV RVDINSPVDP STGSILDDTK IKLHAETIDE ISKKGAKTVV
     LAHQSRPGKK DFTTLQQHAK ALSNILNRPV DYIDDIFGTA AREEIKRLKK GDILLLENVR
     FYPEEILKRD PHQQAETHMV RKLYPIIDIF INDAFAAAHR SQPSLVGFAV KLPSGAGRIM
     EKELKSLYGA VDNAEKPCVY VLGGVKVDDS IMVLENVLRN GSADYVLTTG LVANIFLWAS
     GINLGKYNED FIINKGYIDF VEKGKQLLEE FDGQIKMPDD VAVCVDNARV EYCTKNIPNK
     PIYDIGTNTI TEYAKFIRDA KTIFANGPAG VFEQEGFSIG TEDILNTIAS SNGYSIIGGG
     HLAAAANQMG LSSGITHISS GGGASINLLA GEKLPVVEIL TEVKMKGRK