ID   PGK_CONMG               Reviewed;         378 AA.
AC   O00940;
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   Condylostoma magnum.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Condylostomatidae; Condylostoma.
OX   NCBI_TaxID=40633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Pearlman R.E.;
RL   Submitted (APR-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; U97356; AAB58163.1; -; Genomic_DNA.
DR   AlphaFoldDB; O00940; -.
DR   SMR; O00940; -.
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; 3.
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..>378
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145847"
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         288
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         349..352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         378
SQ   SEQUENCE   378 AA;  40900 MW;  0422A6693EE1328C CRC64;
     VDFNVPIKDG RITDSNRIQA TLPSIQAVLD NGAKSLVLMS HLGRPDGRRD EKSSLRPVAE
     QLQTLLGRPV TFLEDCVGPE IESACADPAP GSVFLLENLR FHPEEEGAGV DESGNKFKPS
     QEQVQTFRDS LTRLGDVYIN DAFGTAHRAH SSMAGINLPQ RAAGYLMGKE LEYFSRALEN
     PNRPLLVIMG GAKVSDKIQL INNLLDNCNE MIIAGGMAFT FKKVLDNLEI GNSLFDEAGA
     KIVQGIIDKA AERHVQIHLP TDFVCGDKFE TGCNVQTYSG NIPEGFMGLD IGPELQEAMA
     QAIQRAETIV WNGPPGVFEI PEFRAGSERF FREIVAATRD RRVVSIVGGG DTAAFAKTMG
     DESDVISHIS TGGGASDP
//