ID   PGK_PARPR               Reviewed;         367 AA.
AC   O00869;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
DE   Flags: Fragment;
GN   Name=PGK;
OS   Paramecium primaurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5886;
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; AF001849; AAB58241.1; -; Genomic_DNA.
DR   AlphaFoldDB; O00869; -.
DR   SMR; O00869; -.
DR   PRIDE; O00869; -.
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   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..>367
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145858"
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         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
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         367
SQ   SEQUENCE   367 AA;  39876 MW;  DEF64500127DE460 CRC64;
     VDFNVPIKEG KVKNTTRIQG AIPTLKKILE QNPKNVTLMS HMGRPDGKRV EKDSLKIVVP
     KLEELLGTKV NFVNDCVGSE ALEASNAGNG QINLLENLRF HIQEEGKGLD ANGAKIKADK
     ESVKKFRKEL SSLGDIYVND AFGTAHRAHS SMVGIDHKIR VAGYLMKKEL DYFAKALETP
     QRPFLVILGG AKVADKIQLI KSMLDKVDEM IIGGGMAFTF LKKYIMFPIG KSLFDEEGYK
     IVDEIIAKAK EKNVKIHLPT DFVCGTGLDA SSPVALHDLK SGIPDGWLGL DAGQLTQREN
     ADAIGRAKTI VWNGPQGAFE IEQFKNGSVS MLNALVKQTQ NGATTIVGGG DTVNLVGANK
     ANDKLSH