G3PG_LEIME
ID G3PG_LEIME Reviewed; 361 AA.
AC Q27890;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, glycosomal;
DE Short=GAPDH;
DE EC=1.2.1.12;
GN Name=GAPG;
OS Leishmania mexicana.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5665;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1435864; DOI=10.1016/0166-6851(92)90132-4;
RA Hannaert V., Blaauw M., Kohl L., Allert S., Opperdoes F.R., Michels P.A.M.;
RT "Molecular analysis of the cytosolic and glycosomal glyceraldehyde-3-
RT phosphate dehydrogenase in Leishmania mexicana.";
RL Mol. Biochem. Parasitol. 55:115-126(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD AND INORGANIC
RP PHOSPHATE, AND SUBUNIT.
RX PubMed=7578111; DOI=10.1021/bi00046a004;
RA Kim H., Feil I.K., Verlinde C.L.M.J., Petra P.H., Hol W.G.J.;
RT "Crystal structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase
RT from Leishmania mexicana: implications for structure-based drug design and
RT a new position for the inorganic phosphate binding site.";
RL Biochemistry 34:14975-14986(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD AND INORGANIC
RP PHOSPHATE, AND SUBUNIT.
RX PubMed=9571030; DOI=10.1006/jmbi.1998.1661;
RA Kim H., Hol W.G.J.;
RT "Crystal structure of Leishmania mexicana glycosomal glyceraldehyde-3-
RT phosphate dehydrogenase in a new crystal form confirms the putative
RT physiological active site structure.";
RL J. Mol. Biol. 278:5-11(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH ADENOSINE ANALOGS.
RX PubMed=10200252; DOI=10.1073/pnas.96.8.4273;
RA Aronov A.M., Suresh S., Buckner F.S., van Voorhis W.C., Verlinde C.L.,
RA Opperdoes F.R., Hol W.G.J., Gelb M.H.;
RT "Structure-based design of submicromolar, biologically active inhibitors of
RT trypanosomatid glyceraldehyde-3-phosphate dehydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4273-4278(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ADENOSINE ANALOGS,
RP AND SUBUNIT.
RX PubMed=11371162; DOI=10.1006/jmbi.2001.4588;
RA Suresh S., Bressi J.C., Kennedy K.J., Verlinde C.L.M.J., Gelb M.H.,
RA Hol W.G.J.;
RT "Conformational changes in Leishmania mexicana glyceraldehyde-3-phosphate
RT dehydrogenase induced by designed inhibitors.";
RL J. Mol. Biol. 309:423-435(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10200252,
CC ECO:0000269|PubMed:11371162, ECO:0000269|PubMed:7578111,
CC ECO:0000269|PubMed:9571030}.
CC -!- SUBCELLULAR LOCATION: Glycosome.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X65226; CAA46334.1; -; Genomic_DNA.
DR EMBL; X65226; CAA46333.1; -; Genomic_DNA.
DR PIR; A48445; A48445.
DR PDB; 1A7K; X-ray; 2.80 A; A/B/C/D=2-361.
DR PDB; 1GYP; X-ray; 2.80 A; A/B/C/D=2-359.
DR PDB; 1GYQ; X-ray; 3.40 A; A/B/C/D=2-359.
DR PDB; 1I32; X-ray; 2.60 A; A/B/C/D/E/F=2-361.
DR PDB; 1I33; X-ray; 3.00 A; A/B/C/D/E/F=2-361.
DR PDBsum; 1A7K; -.
DR PDBsum; 1GYP; -.
DR PDBsum; 1GYQ; -.
DR PDBsum; 1I32; -.
DR PDBsum; 1I33; -.
DR AlphaFoldDB; Q27890; -.
DR SMR; Q27890; -.
DR VEuPathDB; TriTrypDB:LmxM.29.2980; -.
DR BRENDA; 1.2.1.12; 2951.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; Q27890; -.
DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycolysis; Glycosome; NAD; Oxidoreductase; Peroxisome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..361
FT /note="Glyceraldehyde-3-phosphate dehydrogenase,
FT glycosomal"
FT /id="PRO_0000145529"
FT MOTIF 359..361
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 167
FT /note="Nucleophile"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7578111,
FT ECO:0000269|PubMed:9571030"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7578111,
FT ECO:0000269|PubMed:9571030"
FT BINDING 92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7578111,
FT ECO:0000269|PubMed:9571030"
FT BINDING 135
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7578111,
FT ECO:0000269|PubMed:9571030"
FT BINDING 166..168
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 227..228
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7578111,
FT ECO:0000269|PubMed:9571030"
FT SITE 195
FT /note="Activates thiol group during catalysis"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1I32"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:1I32"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1GYP"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1I32"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1I32"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:1GYP"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1I32"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:1I32"
FT TURN 284..289
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:1I32"
FT STRAND 325..334
FT /evidence="ECO:0007829|PDB:1I32"
FT HELIX 338..357
FT /evidence="ECO:0007829|PDB:1I32"
SQ SEQUENCE 361 AA; 39033 MW; 01B116A02CD7D3B5 CRC64;
MAPIKVGING FGRIGRMVFQ AICDQGLIGT EIDVVAVVDM STNAEYFAYQ MKHDTVHGRP
KYTVEAVKSS PSVETADVLV VNGHRIKCVK AQRNPADLPW GKLGVDYVIE STGLFTDKLK
AEGHIKGGAK KVVISAPASG GAKTIVMGVN QHEYSPASHH VVSNASCTTN CLAPIVHVLT
KENFGIETGL MTTIHSYTAT QKTVDGVSLK DWRGGRAAAV NIIPSTTGAA KAVGMVIPST
KGKLTGMSFR VPTPDVSVVD LTFRATRDTS IQEIDKAIKK AAQTYMKGIL GFTDEELVSA
DFINDNRSSV YDSKATLQNN LPGEKRFFKV VSWYDNEWAY SHRVVDLVRY MAAKDAASSK
M
