ID Q95NP3_TRYCR Unreviewed; 430 AA.
AC Q95NP3;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Trypanothione reductase {ECO:0000313|EMBL:AAK71199.1};
DE Flags: Fragment;
GN Name=TR {ECO:0000313|EMBL:AAK71199.1};
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693 {ECO:0000313|EMBL:AAK71199.1};
RN [1] {ECO:0000313|EMBL:AAK71199.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CUICA cl1 {ECO:0000313|EMBL:AAK71199.1}, and SC13
RC {ECO:0000313|EMBL:AAK71205.1};
RX PubMed=11416213; DOI=10.1073/pnas.121187198;
RA Machado C.A., Ayala F.J.;
RT "Nucleotide sequences provide evidence of genetic exchange among distantly
RT related lineages of Trypanosoma cruzi.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7396-7401(2001).
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; AF358981; AAK71199.1; -; Genomic_DNA.
DR EMBL; AF358987; AAK71205.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95NP3; -.
DR VEuPathDB; TriTrypDB:BCY84_10688; -.
DR VEuPathDB; TriTrypDB:C3747_19g298; -.
DR VEuPathDB; TriTrypDB:C4B63_14g241; -.
DR VEuPathDB; TriTrypDB:ECC02_012776; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_3549; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0014700; -.
DR VEuPathDB; TriTrypDB:TcCL_NonESM02890; -.
DR VEuPathDB; TriTrypDB:TcCLB.503555.30; -.
DR VEuPathDB; TriTrypDB:TCDM_11669; -.
DR VEuPathDB; TriTrypDB:TcG_08092; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_004807; -.
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 7..317
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 337..429
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAK71199.1"
FT NON_TER 430
FT /evidence="ECO:0000313|EMBL:AAK71199.1"
SQ SEQUENCE 430 AA; 47271 MW; 910C7B6C19B690F0 CRC64;
TLYKKRVAVI DVQMVHGPPF FSALGGTCVN VGCVPKKLMV TGAQYMEHLR ESAGFGWEFD
RTTLRAEWKK LIAVKDEAVL NINKSYDEMF RDTEGLEFFL GWGSLESKNV VNVRESADPA
SAVKERLETE HILLASGSWP HMPNIPGIEH CISSNEAFYL PEPPRRVLTV GGGFISVEFA
GIFNAYKPKD GQVTLCYRGE MILRGFDHTL REELTKQLTA NGIQILTKEN PAKVELNADG
SKSVTFESGK KMDFDLVMMA IGRSPRTKDL QLQNAGVMIK DGGVQVDEYS RTNVSNIYAI
GDVTNRVMLT PVAINEAAAL VDTVFGTTPR KTDHTRVASA VFSIPPIGTC GLIEEVASKR
YEVVAVYLSS FTPLMHKVSG SKYKTFVAKI ITNHSDGTVL GVHLLGDNAP EIIQGIGICL
KLNAKISDFY
//
