TYTR_TRYBB
ID TYTR_TRYBB Reviewed; 492 AA.
AC P39051;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
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 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=ILTAT 1.1;
RX PubMed=1453951; DOI=10.1111/j.1365-2958.1992.tb01766.x;
RA Aboagye-Kwarteng T., Smith K., Fairlamb A.H.;
RT "Molecular characterization of the trypanothione reductase gene from
RT Crithidia fasciculata and Trypanosoma brucei: comparison with other
RT flavoprotein disulphide oxidoreductases with respect to substrate
RT specificity and catalytic mechanism.";
RL Mol. Microbiol. 6:3089-3099(1992).
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; X63188; CAA44870.1; -; Genomic_DNA.
DR PIR; S28003; S28003.
DR PDB; 2WBA; X-ray; 2.30 A; A/B=1-492.
DR PDBsum; 2WBA; -.
DR AlphaFoldDB; P39051; -.
DR SMR; P39051; -.
DR BindingDB; P39051; -.
DR ChEMBL; CHEMBL1837; -.
DR DrugCentral; P39051; -.
DR BRENDA; 1.8.1.12; 6519.
DR EvolutionaryTrace; P39051; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Redox-active center.
FT CHAIN 1..492
FT /note="Trypanothione reductase"
FT /id="PRO_0000067990"
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"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:2WBA"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 57..75
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 92..116
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 216..227
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:2WBA"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 335..349
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 379..385
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 387..396
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 399..404
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:2WBA"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 423..431
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 434..446
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 451..455
FT /evidence="ECO:0007829|PDB:2WBA"
FT HELIX 465..469
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:2WBA"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:2WBA"
SQ SEQUENCE 492 AA; 53284 MW; FFCA2F11B66F7FF4 CRC64;
MSKIFDLVVI GAGSGGLEAG WNAATLYKKR VAVIDVQTHH GPPHYAALGG TCVNVGCVPK
KLMVTGAQYM DHLRESAGFG WEFDGSSVKA NWKKLIAAKN EAVLDINKSY EGMFNDTEGL
DFFLGWGSLE SKNVVVVRET ADPKSAVKER LQADHILLAT GSWPQMPAIP GVEHCISSNE
AFYLPEPPRR VLTVGGGFIS VEFAGIFNAY KPPGGKVTLC YRNNLILRGF DETIREEVTK
QLTANGIEIM TNENPAKVSL NTDGSKHVTF ESGKTLDVDV VMMAIGRIPR TNDLQLGNVG
VKLTPKGGVQ VDEFSRTNVP NIYAIGDITD RLMLTPVAIN EGAALVDTVF GNKPRKTDHT
RVASAVFSIP PIGTCGLIEE VAAKEFEKVA VYMSSFTPLM HNISGSKYKK FVAKIVTNHS
DGTVLGVHLL GDGAPEIIQA VGVCLRLNAK ISDFYNTIGV HPTSAEELCS MRTPSYYYLK
GEKMETLPES SL
