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   25-NOV-2008, entry version 60.
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; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania.
OX   NCBI_TaxID=5661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/ET/67/HU3;
RX   MEDLINE=95021506; 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
RT   donovani gene encoding trypanothione reductase.";
RL   Mol. Biochem. Parasitol. 64:293-301(1994).
CC   -!- FUNCTION: Trypanothione is the parasite analog of glutathione;
CC       this enzyme is the equivalent of glutathione reductase.
CC   -!- CATALYTIC ACTIVITY: Trypanothione + NADP(+) = trypanothione
CC       disulfide + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
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.
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DR   EMBL; Z23135; CAA80668.1; -; Genomic_DNA.
DR   PIR; S34376; S34376.
DR   HSSP; P39040; 1TYT.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0015042; F:trypanothione-disulfide reductase activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   InterPro; IPR001864; Trypnth_redctse.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   PRINTS; PR00470; TRYPANRDTASE.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01423; trypano_reduc; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    491       Trypanothione reductase.
FT                                /FTId=PRO_0000067989.
FT   NP_BIND      35     52       FAD (By similarity).
FT   ACT_SITE    461    461       Proton acceptor (By similarity).
FT   DISULFID     52     57       Redox-active (By similarity).
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
//