ID   PGK_GLACH               Reviewed;         376 AA.
AC   O00852;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-MAY-2023, entry version 81.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
DE   Flags: Fragment;
GN   Name=PGK;
OS   Glaucoma chattoni.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Glaucomidae; Glaucoma.
OX   NCBI_TaxID=5883;
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; AF001850; AAB58242.1; -; Genomic_DNA.
DR   AlphaFoldDB; O00852; -.
DR   SMR; O00852; -.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF0; PHOSPHOGLYCERATE KINASE; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           <1..>376
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145852"
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         376
SQ   SEQUENCE   376 AA;  40873 MW;  A25D27DC6173DDA9 CRC64;
     VDFNVPLKEG VVKDPTRIAG SIPSIKKILE TNPRGLVLMS HLGRPDGQRV EKHSLKPVLP
     KLEELLGTKV TFLNDCVGKD VEEAVKSSRN GEIILLENLR FHIEEEGKAV DAAGNKVKAD
     PKAVKEFRKS LTNLGDLFFN DAFGTAHRAH SSMVGVDHKI RVAGYLLKKE LEYFSKALES
     PTLPFCVVLG GAKVKDKIQL INSMLDNVNE MIIGGGMAFT FLKRLHNLEI GNSLFDEEGY
     KIVDELLEKA KKKNVKIHLP VDFLCGDSLE ANANTAIHDL QSGIPKGWIG LDAGPKTIAL
     NAEVIARANT IVWNGPQGRF EVDKFRNGSS DLLKKVIERT KTGATSIIGG GDTVNLVQQE
     KASNKVSHVS TGGGAS
//