ID PGK1_TRYCO Reviewed; 420 AA. AC P41760; P41761; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 88. DE RecName: Full=Phosphoglycerate kinase, cytosolic; DE EC=2.7.2.3 {ECO:0000250|UniProtKB:P00558}; GN Name=C1PGK; GN and GN Name=C2PGK; OS Trypanosoma congolense. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas. OX NCBI_TaxID=5692; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=IL3000; RX PubMed=7770090; DOI=10.1016/0166-6851(94)00208-5; RA Parker H.L., Hill T., Alexander K.A., Murphy N.B., Fish W.R., Parsons M.; RT "Three genes and two isozymes: gene conversion and the compartmentalization RT and expression of the phosphoglycerate kinases of Trypanosoma (Nannomonas) RT congolense."; RL Mol. Biochem. Parasitol. 69:269-279(1995). 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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P07378}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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; L37337; AAC37222.1; -; Genomic_DNA. DR EMBL; L37337; AAC37223.1; -; Genomic_DNA. DR EMBL; L37336; AAC37224.1; -; Genomic_DNA. DR EMBL; L37336; AAC37225.1; -; Genomic_DNA. DR AlphaFoldDB; P41760; -. DR SMR; P41760; -. DR VEuPathDB; TriTrypDB:TcIL3000.A.H_000275200; -. DR VEuPathDB; TriTrypDB:TcIL3000.A.H_000275300; -. DR VEuPathDB; TriTrypDB:TcIL3000_1_220; -. DR OMA; YAIPDGW; -. DR UniPathway; UPA00109; UER00185. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0043531; F:ADP binding; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:TreeGrafter. DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB. DR GO; GO:0006094; P:gluconeogenesis; IEA:TreeGrafter. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR CDD; cd00318; Phosphoglycerate_kinase; 1. DR FunFam; 3.40.50.1260:FF:000007; Phosphoglycerate kinase; 1. DR FunFam; 3.40.50.1260:FF:000011; Phosphoglycerate kinase; 1. DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2. DR HAMAP; MF_00145; Phosphoglyc_kinase; 1. DR InterPro; IPR027250; Pgk_euglenozoa. 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:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1. DR Pfam; PF00162; PGK; 1. DR PIRSF; PIRSF000724; Pgk; 1. DR PIRSF; PIRSF500126; Pgk_euglenozoa; 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; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Transferase. FT CHAIN 1..420 FT /note="Phosphoglycerate kinase, cytosolic" FT /id="PRO_0000145867" FT BINDING 23 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 24 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 25 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 26 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 39 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 61 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 62 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 64 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 65 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 135 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 171 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 172 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 217 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 217 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 219 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 219 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 222 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 222 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 223 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 223 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 223 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 241 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 241 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 242 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 242 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 314 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 314 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 314 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 338 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 339 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 344 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 344 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 345 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 345 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 345 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 377 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 377 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 377 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 378 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 378 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" SQ SEQUENCE 420 AA; 44897 MW; 0FE519E5EC184061 CRC64; MTLNEKKSIN ECDLKGKKTL VRVDFNVPVK GGVITNDYRI RSALPTIQKV LNEGGSCILM SHLGRPKGIS ISEAAAVRSA GKVPGYEEAA TLRPVAQRLG ELLSKPVVFA PDCLDAADVV KKMSPGDVVL LENVRFYREE GSKKEEEREA MAKVLASYGD IFVSDAFGTA HRDSATMTGI PKVLGHGAAG YLMEKEISYF SKVLGNPPRP LVAIVGGSKV SDKIQLLDNM LQRIDYLLIG GAMAYTFLKA QGHRIGTSMC EEDRLDLARS LLKKAEDRKV QVLLPVDHVC HTEFKAVDTP VVTADADIPD GHMALDIGPK TIANYVETIG KCKSAIWNGP MGVFEMTPYS KGTFAVAKAM GDCTQKNGLM SIIGGGDSAS AAEQSGEATR MSHVSTGGGA SLELLEGKTL PGVAILDEKV //