ID PGK1_PANTR Reviewed; 417 AA. AC A5A6K4; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 24-JAN-2024, entry version 82. DE RecName: Full=Phosphoglycerate kinase 1; DE EC=2.7.2.3; GN Name=PGK1; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013; RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.; RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils RT large potential divergence of the transcriptome."; RL Gene 399:1-10(2007). CC -!- FUNCTION: Catalyzes one of the two ATP producing reactions in the CC glycolytic pathway via the reversible conversion of 1,3- CC diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a CC glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha CC cofactor protein (primer recognition protein). May play a role in sperm CC motility. {ECO:0000250|UniProtKB:P00558}. 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 Evidence={ECO:0000250|UniProtKB:P00558}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000250|UniProtKB:P00558}. CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00558}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; AB222132; BAF62377.1; -; mRNA. DR RefSeq; NP_001129210.1; NM_001135738.1. DR AlphaFoldDB; A5A6K4; -. DR SMR; A5A6K4; -. DR STRING; 9598.ENSPTRP00000031205; -. DR PaxDb; 9598-ENSPTRP00000058851; -. DR GeneID; 473678; -. DR KEGG; ptr:473678; -. DR CTD; 5230; -. DR eggNOG; KOG1367; Eukaryota. DR InParanoid; A5A6K4; -. DR OrthoDB; 5477183at2759; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000002277; Unplaced. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0043531; F:ADP binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. 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:SF14; PHOSPHOGLYCERATE KINASE 1; 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 2: Evidence at transcript level; KW Acetylation; ATP-binding; Cytoplasm; Glycolysis; Hydroxylation; Kinase; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P00558" FT CHAIN 2..417 FT /note="Phosphoglycerate kinase 1" FT /id="PRO_0000295304" FT BINDING 24..26 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 39 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 63..66 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 123 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 171 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 220 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 313 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 344 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 373..376 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 6 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P09411" FT MOD_RES 11 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 48 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 48 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09411" FT MOD_RES 75 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 76 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P09411" FT MOD_RES 86 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 91 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P09411" FT MOD_RES 97 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 97 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 131 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 131 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000250" FT MOD_RES 146 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 191 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P09411" FT MOD_RES 196 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 199 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 203 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 216 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 220 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 267 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 291 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 323 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 361 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P09411" SQ SEQUENCE 417 AA; 44615 MW; B5DFC7B5FA01767C CRC64; MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL MSHLGRPDGV PMPDKYSLEP VAVELKSLLG KDVLFLKDCV GPEVEKACAN PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN MEIGTSLFDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ ATVASGIPAG WMGLDCGPES SKKYAEAVTR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNI //