ID PGKC_CRIFA Reviewed; 455 AA. AC P08967; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 02-SEP-2026, entry version 104. DE RecName: Full=Phosphoglycerate kinase, glycosomal; DE Short=Phosphoglycerate kinase C; DE EC=2.7.2.3 {ECO:0000250|UniProtKB:P00558}; GN Name=PGKC; Synonyms=PGK-C; OS Crithidia fasciculata. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia. OX NCBI_TaxID=5656; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3402434; DOI=10.1002/j.1460-2075.1988.tb02926.x; RA Swinkels B.W., Evers R., Borst P.; RT "The topogenic signal of the glycosomal (microbody) phosphoglycerate kinase RT of Crithidia fasciculata resides in a carboxy-terminal extension."; RL EMBO J. 7:1159-1165(1988). 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: Glycosome. CC -!- DOMAIN: This glycosomal PGK has a C-terminal extension of 38 AA which CC is not present in the cytosolic isoenzyme. This domain most likely CC serves as topogenic signal to direct the glycosomal PKG to the CC glycosome. 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; X07459; CAA30342.1; -; Genomic_DNA. DR PIR; S00487; TVCRGG. DR AlphaFoldDB; P08967; -. DR SMR; P08967; -. DR VEuPathDB; TriTrypDB:CFAC1_180006900; -. DR UniPathway; UPA00109; UER00185. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell. 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:000001; 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; Glycolysis; Glycosome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Peroxisome; Transferase. FT CHAIN 1..455 FT /note="Phosphoglycerate kinase, glycosomal" FT /id="PRO_0000145850" FT REGION 417..455 FT /note="Topogenic signal" FT /evidence="ECO:0000255" 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 132 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 168 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 169 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 214 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 214 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 215 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 215 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 215 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 215 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 216 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 216 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 219 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 219 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 220 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 220 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" 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 238 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 238 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 239 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 239 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 311 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 311 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 311 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 335 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 336 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 341 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 341 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 342 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 342 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 342 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 374 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 374 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 374 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" FT BINDING 375 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P07378" FT BINDING 375 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q7SIB7" SQ SEQUENCE 455 AA; 47843 MW; D8BF53AE5A0E1BFE CRC64; MSLVPKKSID DAVVKGKKVL IRVDFNVPVK NGEITNDFRI RSALPTIQKV LKEGGSCILM SHLGRPKGAK MSDPKPAKSV RGYEEAATLR PVAARLSELL GQKVEFAPDC LDAASYAAKL KGGDVLLLEN VRFYAEEGSK KEEERDAMAK VLAAYGDVYV SDAFGTAHRD SADMTGIPKV LGAGYAGYLM EKEINYFAQV LNNPPRPLVA IVGGAKVSDK IQLLDNMLGR INYLVIGGAM AYTFQKAQGH AIGISMCEED KLDLAKSLLK KAQERNVEVL LPVDHVCNKE FQGVDAPLVT KDVEIPEGYM ALDIGPKTIK IYEDVIAKCK STIWNGPMGV FEMPCYSKGT FAVAKAMGNG TQKNGLMSII GGGDTASAAE LSGEAKNMSH VSTGGGASLE LLEGKSLPGV TVLTNKDAKA PAAAAAAGGD CPCGSGCAAV PAAATATVSM VLASP //