PGKC_TRYBB
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-AUG-2022, entry version 120.
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}.
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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 CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 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; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PIRSF; PIRSF500126; Pgk_euglenozoa; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 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
