ID PGKC_TRYBB Reviewed; 440 AA. AC P07378; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 03-MAY-2023, entry version 123. DE RecName: Full=Phosphoglycerate kinase, glycosomal; DE Short=Phosphoglycerate kinase C; DE EC=2.7.2.3; OS Trypanosoma brucei brucei. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Trypanosoma. OX NCBI_TaxID=5702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES 2 AND 4). RX PubMed=3267227; DOI=10.1016/0022-2836(88)90534-7; RA le Blancq S.M., Swinkels B.W., Gibson W.C., Borst P.; RT "Evidence for gene conversion between the phosphoglycerate kinase genes of RT Trypanosoma brucei."; RL J. Mol. Biol. 200:439-447(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3004970; DOI=10.1002/j.1460-2075.1985.tb04152.x; RA Osinga K.A., Swinkels B.W., Gibson W.C., Borst P., Veeneman G.H., RA van Boom J.H., Michels P.A.M., Opperdoes F.R.; RT "Topogenesis of microbody enzymes: a sequence comparison of the genes for RT the glycosomal (microbody) and cytosolic phosphoglycerate kinases of RT Trypanosoma brucei."; RL EMBO J. 4:3811-3817(1985). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 5-417 IN COMPLEX WITH ATP AND RP SUBSTRATE. RX PubMed=9000079; DOI=10.1038/385275a0; RA Bernstein B.E., Michels P.A.M., Hol W.G.J.; RT "Synergistic effects of substrate-induced conformational changes in RT phosphoglycerate kinase activation."; RL Nature 385:275-278(1997). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 5-419 IN COMPLEX WITH ADP AND RP SUBSTRATE. RX PubMed=9642090; DOI=10.1006/jmbi.1998.1835; RA Bernstein B.E., Williams D.M., Bressi J.C., Kuhn P., Gelb M.H., RA Blackburn G.M., Hol W.G.J.; RT "A bisubstrate analog induces unexpected conformational changes in RT phosphoglycerate kinase from Trypanosoma brucei."; RL J. Mol. Biol. 279:1137-1148(1998). 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:0000269|PubMed:9642090}. CC -!- SUBCELLULAR LOCATION: Glycosome. CC -!- MISCELLANEOUS: In T.brucei, three genes code for phosphoglycerate CC kinase isozymes, which are transported to different cell compartments. 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; X03370; CAA27069.1; -; Genomic_DNA. DR EMBL; X05889; CAA29318.1; -; Genomic_DNA. DR EMBL; X05890; CAA29321.1; -; Genomic_DNA. DR PIR; B25119; KIUTGG. DR PIR; S02235; TVUTGB. DR PDB; 13PK; X-ray; 2.50 A; A/B/C/D=5-417. DR PDB; 16PK; X-ray; 1.60 A; A=5-417. DR PDBsum; 13PK; -. DR PDBsum; 16PK; -. DR AlphaFoldDB; P07378; -. DR SMR; P07378; -. DR ChEMBL; CHEMBL1741167; -. DR BRENDA; 2.7.2.3; 6519. DR SABIO-RK; P07378; -. DR UniPathway; UPA00109; UER00185. DR EvolutionaryTrace; P07378; -. DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell. 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; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Glycolysis; Glycosome; Kinase; KW Nucleotide-binding; Peroxisome; Transferase. FT CHAIN 1..440 FT /note="Phosphoglycerate kinase, glycosomal" FT /id="PRO_0000145866" FT BINDING 24..26 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9000079, FT ECO:0007744|PDB:13PK" FT BINDING 39 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9000079, FT ECO:0000269|PubMed:9642090, ECO:0007744|PDB:13PK" FT BINDING 62..65 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9000079, FT ECO:0007744|PDB:13PK" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9000079, FT ECO:0000269|PubMed:9642090, ECO:0007744|PDB:13PK" FT BINDING 172 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9000079, FT ECO:0000269|PubMed:9642090, ECO:0007744|PDB:13PK" FT BINDING 223 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:9000079, FT ECO:0007744|PDB:13PK" FT BINDING 338 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:9000079, FT ECO:0007744|PDB:13PK" FT BINDING 345 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:9000079, FT ECO:0007744|PDB:13PK" FT BINDING 375..378 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:9000079, FT ECO:0007744|PDB:13PK" FT VARIANT 75 FT /note="G -> D (in allele 4)" FT HELIX 9..11 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 18..23 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 38..52 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 71..73 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 74..79 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 93..103 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 117..121 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 138..141 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 145..156 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:16PK" FT TURN 175..178 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 179..184 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 191..204 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 209..215 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 221..223 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 224..230 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 235..239 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 243..251 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 265..277 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 286..295 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 313..317 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 319..329 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 333..339 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 347..349 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 351..367 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 376..384 FT /evidence="ECO:0007829|PDB:16PK" FT TURN 388..390 FT /evidence="ECO:0007829|PDB:16PK" FT STRAND 391..394 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 398..405 FT /evidence="ECO:0007829|PDB:16PK" FT HELIX 411..414 FT /evidence="ECO:0007829|PDB:16PK" SQ SEQUENCE 440 AA; 47119 MW; EF95775C216ABDC3 CRC64; MTLNEKKSIN ECDLKGKKVL IRVDFNVPVK NGKITNDYRI RSALPTLKKV LTEGGSCVLM SHLGRPKGIP MAQAGKIRST GGVPGFQQKA TLKPVAKALS ELLLRPVTFA PDCLNAADVV SKMSPGDVVL LENVRFYKEE GSKKAKDREA MAKILASYGD VYISDAFGTA HRDSATMTGI PKILGNGAAG YLMEKEISYF AKVLGNPPRP LVAIVGGAKV SDKIQLLDNM LQRIDYLLIG GAMAYTFLKA QGYSIGKSKC EESKLEFARS LLKKAEDRKV QVILPIDHVC HTEFKAVDSP LITEDQNIPE GHMALDIGPK TIEKYVQTIG KCKSAIWNGP MGVFEMVPYS KGTFAIAKAM GRGTHEHGLM SIIGGGDSAS AAELSGEAKR MSHVSTGGGA SLELLEGKTL PGVTVLDEKS AVVSYASAGT GTLSNRWSSL //