NTRA_ORYSJ
ID NTRA_ORYSJ Reviewed; 368 AA.
AC Q69PS6; Q0DCH8;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Thioredoxin reductase NTRA;
DE EC=1.8.1.9;
DE AltName: Full=NADPH-dependent thioredoxin reductase A;
DE Short=OsNTRA;
GN OrderedLocusNames=Os06g0327300, LOC_Os06g22140; ORFNames=OSJNBb0039F24.13;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Possesses thioredoxin-disulfide reductase activity.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD33510.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF19445.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005477; BAD33510.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008212; BAF19445.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015644379.1; XM_015788893.1.
DR AlphaFoldDB; Q69PS6; -.
DR SMR; Q69PS6; -.
DR STRING; 39947.Q69PS6; -.
DR PaxDb; Q69PS6; -.
DR PRIDE; Q69PS6; -.
DR GeneID; 4340912; -.
DR KEGG; osa:4340912; -.
DR InParanoid; Q69PS6; -.
DR OrthoDB; 1108990at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Electron transport; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Redox-active center; Reference proteome; Transport.
FT CHAIN 1..368
FT /note="Thioredoxin reductase NTRA"
FT /id="PRO_0000394857"
FT BINDING 55..58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 76..77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 84..89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 337..339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT SITE 206
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT SITE 225
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT DISULFID 182..185
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 38218 MW; B31D67E50FCC2FF2 CRC64;
MRLCSKLAAL LRRSRQFAPA AAAASGSATA AAASANGMEE AAAGPLRARV CIIGSGPAAH
TAAVYAARAE LKPVLFEGFL ANDIAAGGQL TTTTDVENFP GFPDGILGAD LMDRCRAQSV
RFGTRILTET VTAVDLSSRP FRVASGDTVV HADAVVVATG AVARRLHFAG SDAFWNRGIS
ACAVCDGAAP IFRNKPIAVV GGGDSAMEEA NFLTKYGSRV YIIHRRNAFR ASKIMQARAL
SNPKIQVVWD SEVVEAYGGA DGGPLAGVKV KNVVSGEVSD LQVAGLFFAI GHEPATKFLG
GQLELDSDGY VVTKPGSTHT SVKGVFAAGD VQDKKYRQAI TAAGSGCMAA LDAEHYLQEI
GAQEDKTD
