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Database: UniProt
Entry: A0A061J4G2_TRYRA
LinkDB: A0A061J4G2_TRYRA
Original site: A0A061J4G2_TRYRA 
ID   A0A061J4G2_TRYRA        Unreviewed;       490 AA.
AC   A0A061J4G2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Trypanothione reductase {ECO:0000256|ARBA:ARBA00013602};
DE            EC=1.8.1.12 {ECO:0000256|ARBA:ARBA00013018};
DE   AltName: Full=N(1),N(8)-bis(glutathionyl)spermidine reductase {ECO:0000256|ARBA:ARBA00029937};
GN   ORFNames=TRSC58_02517 {ECO:0000313|EMBL:ESL09759.1};
OS   Trypanosoma rangeli SC58.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Herpetosoma.
OX   NCBI_TaxID=429131 {ECO:0000313|EMBL:ESL09759.1, ECO:0000313|Proteomes:UP000031737};
RN   [1] {ECO:0000313|EMBL:ESL09759.1, ECO:0000313|Proteomes:UP000031737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC58 {ECO:0000313|EMBL:ESL09759.1,
RC   ECO:0000313|Proteomes:UP000031737};
RA   Stoco P.H., Wagner G., Gerber A., Zaha A., Thompson C., Bartholomeu D.C.,
RA   Luckemeyer D.D., Bahia D., Loreto E., Prestes E.B., Lima F.M.,
RA   Rodrigues-Luiz G., Vallejo G.A., Filho J.F., Monteiro K.M., Tyler K.M.,
RA   de Almeida L.G., Ortiz M.F., Siervo M.A., de Moraes M.H., Cunha O.L.,
RA   Mendonca-Neto R., Silva R., Teixeira S.M., Murta S.M., Sincero T.C.,
RA   Mendes T.A., Urmenyi T.P., Silva V.G., da Rocha W.D., Andersson B.,
RA   Romanha A.J., Steindel M., de Vasconcelos A.T., Grisard E.C.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Trypanothione is the parasite analog of glutathione; this
CC       enzyme is the equivalent of glutathione reductase.
CC       {ECO:0000256|ARBA:ARBA00003667}.
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         Evidence={ECO:0000256|ARBA:ARBA00001054};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESL09759.1}.
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DR   EMBL; AUPL01002517; ESL09759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061J4G2; -.
DR   SMR; A0A061J4G2; -.
DR   EnsemblProtists; ESL09759; ESL09759; TRSC58_02517.
DR   VEuPathDB; TriTrypDB:TRSC58_02517; -.
DR   OrthoDB; 5473641at2759; -.
DR   Proteomes; UP000031737; Unassembled WGS sequence.
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 (NADP) 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; 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; 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   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   PIRSF; PIRSF000350; Mercury_reductase_MerA; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031737}.
FT   DOMAIN          4..340
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          360..466
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        459
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         60
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         126
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         159..161
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         194..201
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         285
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         325
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        51..56
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   490 AA;  53574 MW;  4963250998E88F6C CRC64;
     MKAFDLVVIG AGSGGLEAAW NAATLYKKRV AVIDVQKTHG PPFFSAMGGT CVNVGCVPKK
     LMVTGAQYMD QLRESQGFGW EFDRSTLKAN WSKLIAAKDE AVLDINKSYE GMFEETEGLE
     FFLGWGSLES ATVVNVRETA DSSSAVRERL ETKHIIIATG SWPQMLNIPG IEHCISSNEA
     FYLPEPPRRA LTVGGGFISV EFAGIFNAYK PKDGKVTLCY RRDLILRGFD NTLREELTKQ
     LTANGIDIMT KENPTKVELN PDGSKHVTFE SGKTMDFDVV MMAVGRIPRI NDLQLQNAGV
     VLNKGAVQVD EYSRTNVSNI YAIGDVTQRV MLTPVAINEA SALIDTVFGN KPRKTDHTRV
     ASAVFSIPPI GTCGLTEEAA SKQYDRVAVY LSSFTPLMHN ISGSKYKKFV VKIITNDSDG
     TVIGVHLLGD SAPEIIQAVG ICLKMNAKIS DFYNTIGVHP TSAEELCSMR TPSYYYVKGT
     KTETALEADL
//
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