TRXB2_ARATH
ID TRXB2_ARATH Reviewed; 383 AA.
AC Q39242; F4INH1; O22751; Q0WW76; Q8LPI1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Thioredoxin reductase 2;
DE EC=1.8.1.9;
DE AltName: Full=NADPH-dependent thioredoxin reductase 2;
DE Short=NTR2;
DE AltName: Full=NADPH-dependent thioredoxin reductase A;
DE Short=AtNTRA;
GN Name=NTR2; Synonyms=NTRA; OrderedLocusNames=At2g17420; ORFNames=F5J6.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-383.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-383.
RC TISSUE=Silique;
RX PubMed=8308900; DOI=10.1006/jmbi.1994.1091;
RA Jacquot J.-P., Rivera-Madrid R., Marinho P., Kollarova M., le Marechal P.,
RA Miginiac-Maslow M., Meyer Y.;
RT "Arabidopsis thaliana NAPHP thioredoxin reductase. cDNA characterization
RT and expression of the recombinant protein in Escherichia coli.";
RL J. Mol. Biol. 235:1357-1363(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-383.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11717467; DOI=10.1073/pnas.241340898;
RA Laloi C., Rayapuram N., Chartier Y., Grienenberger J.M., Bonnard G.,
RA Meyer Y.;
RT "Identification and characterization of a mitochondrial thioredoxin system
RT in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14144-14149(2001).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15642341; DOI=10.1016/j.febslet.2004.11.094;
RA Reichheld J.P., Meyer E., Khafif M., Bonnard G., Meyer Y.;
RT "AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis
RT thaliana.";
RL FEBS Lett. 579:337-342(2005).
CC -!- FUNCTION: Possesses thioredoxin-disulfide reductase activity towards
CC thioredoxins O1, O2 and F3. {ECO:0000269|PubMed:11717467}.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15642341}.
CC Mitochondrion matrix {ECO:0000269|PubMed:11717467,
CC ECO:0000269|PubMed:15642341}.
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; CP002685; AEC06623.2; -; Genomic_DNA.
DR EMBL; AK226480; BAE98622.1; -; mRNA.
DR EMBL; Z23108; CAA80655.1; -; mRNA.
DR EMBL; AY099756; AAM20607.1; -; mRNA.
DR PIR; A84552; A84552.
DR PIR; S44026; S44026.
DR RefSeq; NP_179334.5; NM_127297.5.
DR AlphaFoldDB; Q39242; -.
DR SMR; Q39242; -.
DR STRING; 3702.AT2G17420.1; -.
DR iPTMnet; Q39242; -.
DR PaxDb; Q39242; -.
DR PRIDE; Q39242; -.
DR ProteomicsDB; 232450; -.
DR EnsemblPlants; AT2G17420.1; AT2G17420.1; AT2G17420.
DR GeneID; 816248; -.
DR Gramene; AT2G17420.1; AT2G17420.1; AT2G17420.
DR KEGG; ath:AT2G17420; -.
DR Araport; AT2G17420; -.
DR eggNOG; KOG0404; Eukaryota.
DR HOGENOM; CLU_031864_5_1_1; -.
DR InParanoid; Q39242; -.
DR OMA; VDNFPGY; -.
DR OrthoDB; 1108990at2759; -.
DR PhylomeDB; Q39242; -.
DR BioCyc; ARA:AT2G17420-MON; -.
DR BRENDA; 1.8.1.9; 399.
DR PRO; PR:Q39242; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q39242; baseline and differential.
DR Genevisible; Q39242; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; ISA:CACAO.
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 Cytoplasm; Disulfide bond; Electron transport; FAD; Flavoprotein;
KW Mitochondrion; NADP; Oxidoreductase; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..383
FT /note="Thioredoxin reductase 2"
FT /id="PRO_0000166772"
FT BINDING 66..69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 87..88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 95..100
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 352..354
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 197..200
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 89..90
FT /note="GW -> PR (in Ref. 4; CAA80655)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="E -> Q (in Ref. 4; CAA80655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 40635 MW; 1BA9339AE6E66FFE CRC64;
MCWISMSQSR FIIKSLFSTA GGFLLGSALS NPPSLATAFS SSSSSSSAAA AVDMETHKTK
VCIVGSGPAA HTAAIYASRA ELKPLLFEGW MANDIAPGGQ LTTTTDVENF PGFPEGILGI
DIVEKFRKQS ERFGTTIFTE TVNKVDFSSK PFKLFTDSRT VLADSVIIST GAVAKRLSFT
GSGEGNGGFW NRGISACAVC DGAAPIFRNK PLVVIGGGDS AMEEANFLTK YGSKVYIIHR
RDTFRASKIM QQRALSNPKI EVIWNSAVVE AYGDENGRVL GGLKVKNVVT GDVSDLKVSG
LFFAIGHEPA TKFLDGQLEL DEDGYVVTKP GTTKTSVVGV FAAGDVQDKK YRQAITAAGT
GCMAALDAEH YLQEIGSQEG KSD
