ID   GPDA_TRYBB              Reviewed;         354 AA.
AC   P90593;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal;
DE            EC=1.1.1.8;
GN   Name=GPD;
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].
RC   STRAIN=427;
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).
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   -!- SUBCELLULAR LOCATION: Glycosome.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; X89738; CAA61890.1; -; Genomic_DNA.
DR   PIR; T48649; T48649.
DR   AlphaFoldDB; P90593; -.
DR   SMR; P90593; -.
DR   SwissPalm; P90593; -.
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:0042803; F:protein homodimerization activity; 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; IPR017751; G3P_DH_NAD-dep_euk.
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   TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   Glycosome; NAD; Oxidoreductase; Peroxisome.
FT   CHAIN           1..354
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)],
FT                   glycosomal"
FT                   /id="PRO_0000138083"
FT   MOTIF           352..354
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        203
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..20
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         267..268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  37783 MW;  12CE19AEDA9E4EC9 CRC64;
     MVSGVTYLKR GAVFGSGAFG TALACVLAKK CESVSVWHMN ANEARVVNQK HENVYFLPGA
     PLPANLTFTA DAEECAKGAE IVLFVIPTQF LRGFLQKNSH ILRNHVVSRN VPVVMCSKGI
     ERSSLLFPAQ ILEEFLPNYP IGVIAGPSFA IEVAKGMLTN VCTAAADINM ARKIQRIMTT
     SDGSFRCWAT TDVIGCEIAS AMKNVLAIAS GALKGLGTEN NARAALISRG LLEIRDLTLA
     LGGTGEAVFG LPGLGDLLLT CSSELSRNFT VGMKLGQGIS LEEIKRTSKA VAEGVATAEP
     LERLAKKHNA DLPICHEVYN VLYANGCAKR SFKKLNSCKL ADEGLPALPR TSKM