ID PGK_CHICK Reviewed; 417 AA. AC P51903; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 08-NOV-2023, entry version 120. DE RecName: Full=Phosphoglycerate kinase; DE EC=2.7.2.3; GN Name=PGK; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=8182283; DOI=10.1093/oxfordjournals.jhered.a111416; RA Rauen K.A., le Ciel C.D., Abbott U.K., Hutchison N.J.; RT "Localization of the chicken PgK gene to chromosome 4p by fluorescence in RT situ hybridization."; RL J. Hered. 85:147-150(1994). 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}. 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; L37101; AAC42219.1; -; mRNA. DR PIR; I50407; I50407. DR RefSeq; NP_990316.1; NM_204985.2. DR AlphaFoldDB; P51903; -. DR SMR; P51903; -. DR BioGRID; 676107; 2. DR IntAct; P51903; 1. DR STRING; 9031.ENSGALP00000012878; -. DR PaxDb; 9031-ENSGALP00000012878; -. DR GeneID; 395833; -. DR KEGG; gga:395833; -. DR CTD; 5232; -. DR VEuPathDB; HostDB:geneid_395833; -. DR eggNOG; KOG1367; Eukaryota. DR InParanoid; P51903; -. DR PhylomeDB; P51903; -. DR Reactome; R-GGA-352875; Gluconeogenesis. DR Reactome; R-GGA-352882; Glycolysis. DR SABIO-RK; P51903; -. DR UniPathway; UPA00109; UER00185. DR PRO; PR:P51903; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005694; C:chromosome; TAS:AgBase. 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; ISS:UniProtKB. DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB. 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; ISS:UniProtKB. 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 2: Evidence at transcript level; KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..417 FT /note="Phosphoglycerate kinase" FT /id="PRO_0000145841" 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" SQ SEQUENCE 417 AA; 44717 MW; D4C3BEC9D40D5FDA CRC64; MSLSNKLTLD KVDVKGKRVV MRVDFNVPMK DHKITNNQRI KAAVPTIKHC LDHGAKSVVL MSHLGRPDGV PMPDKFSFSP VAVELKALLG REVSFLKDCV GPEVEKACAN PANGSVILLE NLRFHVEEEG KGKDASGNKI KADAAKVEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVH LPQKAAGFLM KKELDYFAKA LESPERPFLA ILGGAKVQDK IQLISNMLDK VNEMIIGGGM AFTFLKVLNN MQIGNSLFDE EGSKIVKDLM AKAEKNGVKI TLPVDFITAD KFDEHAQTGE ATVASGIPAG WMGLDCGPES VKKFVEVVGR AKQIVWNGPV GVFEWDKFSK GTKALMDKVV EVTGKGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSSV //