NTRB_ORYSJ
ID NTRB_ORYSJ Reviewed; 331 AA.
AC Q6ZFU6; A0A0P0VNZ7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Thioredoxin reductase NTRB;
DE EC=1.8.1.9;
DE AltName: Full=NADPH-dependent thioredoxin reductase B;
DE Short=OsNTRB;
GN Name=NTRB; OrderedLocusNames=Os02g0713400, LOC_Os02g48290;
GN ORFNames=OJ1479_B12.9, OsJ_08126;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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}.
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DR EMBL; AP004165; BAD07786.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09825.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80584.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE57677.1; -; Genomic_DNA.
DR EMBL; AK071251; BAG92394.1; -; mRNA.
DR RefSeq; XP_015627135.1; XM_015771649.1.
DR AlphaFoldDB; Q6ZFU6; -.
DR SMR; Q6ZFU6; -.
DR STRING; 4530.OS02T0713400-01; -.
DR PaxDb; Q6ZFU6; -.
DR PRIDE; Q6ZFU6; -.
DR EnsemblPlants; Os02t0713400-01; Os02t0713400-01; Os02g0713400.
DR GeneID; 4330505; -.
DR Gramene; Os02t0713400-01; Os02t0713400-01; Os02g0713400.
DR KEGG; osa:4330505; -.
DR eggNOG; KOG0404; Eukaryota.
DR HOGENOM; CLU_031864_5_1_1; -.
DR InParanoid; Q6ZFU6; -.
DR OMA; VDNFPGY; -.
DR OrthoDB; 1108990at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6ZFU6; OS.
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 2: Evidence at transcript level;
KW Disulfide bond; Electron transport; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Redox-active center; Reference proteome; Transport.
FT CHAIN 1..331
FT /note="Thioredoxin reductase NTRB"
FT /id="PRO_0000394858"
FT BINDING 18..21
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 39..40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 47..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 300..302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT SITE 169
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT SITE 188
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT DISULFID 145..148
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 331 AA; 34676 MW; F02C07ED24BAF9AB CRC64;
MEGSAGAPLR TRVCIIGSGP SAHTAAIYAA RAELKPVLFE GWLANDIAAG GQLTTTTDVE
NFPGFPEGIL GGELMDRCRA QSLRFGTSII SETVTAVDFS ARPFRVASDS TTVLADAVVV
ATGAVARRLH FAGSDAYWNR GISACAVCDG AAPIFRNKPI AVIGGGDSAM EESNFLTKYG
SHVYIIHRRN TFRASKIMQA RALSNPKIQV FWDSEVVEAY GGEGGGPLAG VKVKNLVTGK
ISDLQVSGLF FAIGHEPATK FLGGQLELDA DGYVATKPGS THTSVKGVFA AGDVQDKKYR
QAITAAGSGC MAALDAEHYL QEVGAQEGKA D
