GPDA_LEIME
ID GPDA_LEIME Reviewed; 366 AA.
AC P90551;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal;
DE EC=1.1.1.8;
GN Name=GPD;
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], AND SUBCELLULAR LOCATION.
RX PubMed=8920004; DOI=10.1016/0166-6851(95)02556-1;
RA Kohl L., Drmota T., Thi C.-D., Callens M., van Beeumen J., Opperdoes F.R.,
RA Michels P.A.M.;
RT "Cloning and characterization of the NAD-linked glycerol-3-phosphate
RT dehydrogenases of Trypanosoma brucei brucei and Leishmania mexicana
RT mexicana and expression of the trypanosome enzyme in Escherichia coli.";
RL Mol. Biochem. Parasitol. 76:159-173(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOG, AND SUBUNIT.
RX PubMed=10801498; DOI=10.1016/s0969-2126(00)00135-0;
RA Suresh S., Turley S., Opperdoes F.R., Michels P.A.M., Hol W.G.J.;
RT "A potential target enzyme for trypanocidal drugs revealed by the crystal
RT structure of NAD-dependent glycerol-3-phosphate dehydrogenase from
RT Leishmania mexicana.";
RL Structure 8:541-552(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD ANALOG.
RX PubMed=12445769; DOI=10.1016/s1074-5521(02)00243-0;
RA Choe J., Suresh S., Wisedchaisri G., Kennedy K.J., Gelb M.H., Hol W.G.J.;
RT "Anomalous differences of light elements in determining precise binding
RT modes of ligands to glycerol-3-phosphate dehydrogenase.";
RL Chem. Biol. 9:1189-1197(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NAD,
RP AND MUTAGENESIS OF LYS-125 AND LYS-210.
RX PubMed=12758080; DOI=10.1016/s0022-2836(03)00421-2;
RA Choe J., Guerra D., Michels P.A.M., Hol W.G.J.;
RT "Leishmania mexicana glycerol-3-phosphate dehydrogenase showed
RT conformational changes upon binding a bi-substrate adduct.";
RL J. Mol. Biol. 329:335-349(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.8;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10801498,
CC ECO:0000269|PubMed:12445769, ECO:0000269|PubMed:12758080}.
CC -!- SUBCELLULAR LOCATION: Glycosome {ECO:0000269|PubMed:8920004}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; X89739; CAA61891.1; -; Genomic_DNA.
DR PDB; 1EVY; X-ray; 1.75 A; A=1-366.
DR PDB; 1EVZ; X-ray; 2.80 A; A=1-366.
DR PDB; 1JDJ; X-ray; 2.20 A; A=1-366.
DR PDB; 1M66; X-ray; 1.90 A; A=1-366.
DR PDB; 1M67; X-ray; 2.50 A; A=1-366.
DR PDB; 1N1E; X-ray; 1.90 A; A/B=1-366.
DR PDB; 1N1G; X-ray; 2.50 A; A=1-366.
DR PDBsum; 1EVY; -.
DR PDBsum; 1EVZ; -.
DR PDBsum; 1JDJ; -.
DR PDBsum; 1M66; -.
DR PDBsum; 1M67; -.
DR PDBsum; 1N1E; -.
DR PDBsum; 1N1G; -.
DR AlphaFoldDB; P90551; -.
DR SMR; P90551; -.
DR VEuPathDB; TriTrypDB:LmxM.10.0510; -.
DR SABIO-RK; P90551; -.
DR EvolutionaryTrace; P90551; -.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosome; NAD; Oxidoreductase; Peroxisome.
FT CHAIN 1..366
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)],
FT glycosomal"
FT /id="PRO_0000262292"
FT MOTIF 364..366
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 22..27
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10801498,
FT ECO:0000269|PubMed:12758080"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10801498,
FT ECO:0000269|PubMed:12758080"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12758080"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10801498,
FT ECO:0000269|PubMed:12758080"
FT BINDING 274..275
FT /ligand="substrate"
FT BINDING 274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10801498,
FT ECO:0000269|PubMed:12758080"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10801498,
FT ECO:0000269|PubMed:12758080"
FT MUTAGEN 125
FT /note="K->A,M: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12758080"
FT MUTAGEN 210
FT /note="K->A,M: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12758080"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:1EVY"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1EVY"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:1EVY"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1EVY"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:1EVY"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1EVY"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1EVY"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:1EVY"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1EVY"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:1EVY"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:1EVY"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 200..222
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 227..247
FT /evidence="ECO:0007829|PDB:1EVY"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:1EVY"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 300..315
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 335..342
FT /evidence="ECO:0007829|PDB:1EVY"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1EVY"
SQ SEQUENCE 366 AA; 39272 MW; E47594525FC0CF44 CRC64;
MSTKQHSAKD ELLYLNKAVV FGSGAFGTAL AMVLSKKCRE VCVWHMNEEE VRLVNEKREN
VLFLKGVQLA SNITFTSDVE KAYNGAEIIL FVIPTQFLRG FFEKSGGNLI AYAKEKQVPV
LVCTKGIERS TLKFPAEIIG EFLPSPLLSV LAGPSFAIEV ATGVFTCVSI ASADINVARR
LQRIMSTGDR SFVCWATTDT VGCEVASAVK NVLAIGSGVA NGLGMGLNAR AALIMRGLLE
IRDLTAALGG DGSAVFGLAG LGDLQLTCSS ELSRNFTVGK KLGKGLPIEE IQRTSKAVAE
GVATADPLMR LAKQLKVKMP LCHQIYEIVY KKKNPRDALA DLLSCGLQDE GLPPLFKRSA
STPSKL
