ID   TYTR_LEIDO              Reviewed;         491 AA.
AC   P39050;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Trypanothione reductase;
DE            Short=TR;
DE            EC=1.8.1.12;
DE   AltName: Full=N(1),N(8)-bis(glutathionyl)spermidine reductase;
GN   Name=TPR;
OS   Leishmania donovani.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/ET/67/HU3;
RX   PubMed=7935607; DOI=10.1016/0166-6851(94)00034-4;
RA   Taylor M.C., Kelly J.M., Chapman C.J., Fairlamb A.H., Miles M.A.;
RT   "The structure, organization, and expression of the Leishmania donovani
RT   gene encoding trypanothione reductase.";
RL   Mol. Biochem. Parasitol. 64:293-301(1994).
CC   -!- FUNCTION: Trypanothione is the parasite analog of glutathione; this
CC       enzyme is the equivalent of glutathione reductase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + trypanothione = H(+) + NADPH + trypanothione
CC         disulfide; Xref=Rhea:RHEA:16757, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58290, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58661; EC=1.8.1.12;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; Z23135; CAA80668.1; -; Genomic_DNA.
DR   PIR; S34376; S34376.
DR   AlphaFoldDB; P39050; -.
DR   SMR; P39050; -.
DR   ChEMBL; CHEMBL2176840; -.
DR   KEGG; ag:CAA80668; -.
DR   VEuPathDB; TriTrypDB:LdBPK_050350.1; -.
DR   VEuPathDB; TriTrypDB:LdCL_050008500; -.
DR   VEuPathDB; TriTrypDB:LDHU3_05.0400; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0015042; F:trypanothione-disulfide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001864; Trypnth_redctse.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   PRINTS; PR00470; TRYPANRDTASE.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01423; trypano_reduc; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..491
FT                   /note="Trypanothione reductase"
FT                   /id="PRO_0000067989"
FT   ACT_SITE        461
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         35..52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..57
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   491 AA;  52933 MW;  5A777DA32E8E752A CRC64;
     MSRAYDLVVL GAGSGGLEAG WNAAVTHKKK VAVVDVQATH GPPALVALGG TCVNVGCVPK
     KLMVTGAQYM DLIRESGGFG WEMDRESLCP NWKTLIAAKN KVVNSINESY KSMFADTEGL
     SFHMGFGALQ DAHTVVVRKS EDPHSDVLET LDTEYILIAT GSWPTRLGVP GDEFCITSNE
     AFYLEDAPKR MLCVGGGYIA VEFAGIFNGY KPCGGYVDLC YRGDLILRGF DTEVRKSLTK
     QLGANGIRVR TNLNPTKITK NEDGSNHVHF NDGTEEDYDQ VMLAIGVPRS QALQLDKAGV
     RTGKNGAVQV DAYSKTSVDN IYAIGDVTNR VMLTPVAINE GACVLLETVF GGKPRATDHT
     KVACAVFSIP PIGTCGMTEE EAAKNYETVA VYASSFTPLM HNISGSKHKE FMIRIITNES
     NGEVLGVHML GDSAPEIIQS VGICMKMGAK ISDFHSTIGV HPTSAEELCS MRTPAYFYES
     GKRVEKLSSN L