ID   I6LED5_TRYCR            Unreviewed;       430 AA.
AC   I6LED5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Trypanothione reductase {ECO:0000313|EMBL:AAX40410.1};
DE   Flags: Fragment;
GN   Name=TR {ECO:0000313|EMBL:AAX40410.1};
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693 {ECO:0000313|EMBL:AAX40410.1};
RN   [1] {ECO:0000313|EMBL:AAX40410.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CL Brener {ECO:0000313|EMBL:AAX40410.1};
RA   Tomazi L., Pereira P.M., Briones M.R.S.;
RT   "Phylogenies and polymorphism of Trypanosoma cruzi: new inferences about
RT   rDNA 1/2 e Zymodeme 3 groups.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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DR   EMBL; AY785725; AAX40410.1; -; Genomic_DNA.
DR   AlphaFoldDB; I6LED5; -.
DR   VEuPathDB; TriTrypDB:C3747_19g298; -.
DR   VEuPathDB; TriTrypDB:ECC02_012776; -.
DR   VEuPathDB; TriTrypDB:TcCLB.484299.10; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001864; Trypnth_redctse.
DR   NCBIfam; TIGR01423; trypano_reduc; 1.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 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   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691}.
FT   DOMAIN          6..318
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          338..430
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAX40410.1"
FT   NON_TER         430
FT                   /evidence="ECO:0000313|EMBL:AAX40410.1"
SQ   SEQUENCE   430 AA;  47184 MW;  9DDE1F6A3092FA87 CRC64;
     ATLYKKRVAV IDVQMVHGPP FFSALGGTCV NVGCVPKKLM VTGAQYMEHL RESAGFGWEF
     DRTTLRAEWK KLIAVKDEAV LNINKSYEEM FRDTEGLEFF LGWGSLESKN VVNVRESADP
     ASAVKERLET ENILLASGSW PHMPNILGIE HCISSNEAFY LPEPPRRVLT VGGGFISVEF
     AGIFNAYKPK DGQVTLCYRG EMILRGFDHT LREELTKQLT ANGIQILTKE NPAKVELNAD
     GSKSVTFESG KKMDFDLVMM AIGRSPRTKD LQLQNAGVMI KNGGVQVDEY SRTNVSNIYA
     IGDVTNRVML TPVAINEAAA LVDTVFGTNP RKTDHTRVAS AVFSIPPIGT CGLIEEVASK
     RYEVVAVYLS SFTPLMHNIS GSKYKTFVAK IITNHSDGTV LGVHLLGDNA PEIIQGVGIC
     LKLNAKISDF
//