ID   PGK_TETPY               Reviewed;         375 AA.
AC   O00871;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
DE   Flags: Fragment;
GN   Name=PGK;
OS   Tetrahymena pyriformis.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Pearlman R.E.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AF001851; AAB58243.1; -; Genomic_DNA.
DR   AlphaFoldDB; O00871; -.
DR   SMR; O00871; -.
DR   UniPathway; UPA00109; UER00185.
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; -; 3.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           <1..>375
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145860"
FT   BINDING         2..4
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         290
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         350..353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         375
SQ   SEQUENCE   375 AA;  40673 MW;  141D0ED9620C34DB CRC64;
     VDFNVPLKDG QVKDPTRIQG SIPSIKKILE QNPKGLVLMS HLGRPDGNRV EKHSMKPVVP
     KLEQLLGTKV KFLNDCVGKD VEEAVKSSRN GEIILLENLR FHAEEEGKSI DAAGNKVKAD
     PKAVKEFRKS LTSLGDLYVN DAFGTAHRAH SSMVGVDHKI RAAGYLLKKE LDYFSKALES
     PNRPFLVVLG GAKVKDKIQL IESMIDKVDE MIIGGGMAFT FLKRIHNMEI GNSLFDEEGY
     KIVDQLLEKA KAKGVKIHLP VDFLCGDSLE ANANTQIHDL ISGIPKGWIG LDAGPKTIAL
     NADAVARANT IVWNGPQGRF EVDKFRQGSA DLLKRVSART AAGATSIIGG GDTVNLVQQE
     KATDKVSHVS TGGGE