PGK_STENO
ID PGK_STENO Reviewed; 419 AA.
AC O02609;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=PGK;
OS Sterkiella nova (Ciliate) (Oxytricha nova).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Sterkiella.
OX NCBI_TaxID=200597;
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; AF001848; AAB58240.1; -; Genomic_DNA.
DR AlphaFoldDB; O02609; -.
DR SMR; O02609; -.
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 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; Glycolysis; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..419
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145857"
FT BINDING 25..27
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64..67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 419 AA; 45166 MW; 83B999ECD3B99C7C CRC64;
MLSKKLAIDH IPHLIKGKRV LMRVDFNVPI KEGKIKDLTR IQGALPSINY CLENGAESVV
LMSHLGRPDG QRVEKHSLKP VLPAIEDLLK KKVQFLDDCV GSEVERECKS ASKGKVILLE
NLRFHLAEEG KGVINGEKVK ATKEDIAAFR KSLTSLGELY VNDGFGTAHR AHSSMVGVNV
DTRAAGFLLK KELQYFSKIL ETPERPLTVV MGGAKVADKI QLIMKLLELA DELIIGGGMA
FTFNKVLDGS NIGKSLFDQE GAKIVPDIIK KAKERGVKIH LPVDAVAADK FEESAATQLV
DLKTGAIPDG WMGLDIGPKT IEQNSRVILR AKTVFWNGPQ GVFEMAPFSK GSLSMLDDII
KATQTGATSV AGGGDTVSLL GKVKGTTDKF SHVSTGGGAS LELLQGKQLP GVVALSDRQ
