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-MAY-2023, entry version 77. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 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; 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. 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 //