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
//