TRXB1_ARATH
ID TRXB1_ARATH Reviewed; 375 AA.
AC Q39243; Q84W20; Q9SVW9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Thioredoxin reductase 1, mitochondrial;
DE EC=1.8.1.9 {ECO:0000305|PubMed:11717467, ECO:0000305|PubMed:8308900};
DE AltName: Full=NADPH-dependent thioredoxin reductase 1;
DE Short=NTR1;
DE AltName: Full=NADPH-dependent thioredoxin reductase B;
DE Short=AtNTRB {ECO:0000303|PubMed:11717467};
DE Flags: Precursor;
GN Name=NTR1; Synonyms=NTRB; OrderedLocusNames=At4g35460; ORFNames=F15J1.30;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 [MRNA] OF 12-375, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-375.
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP 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 [6]
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-37.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 43-375 IN COMPLEX WITH FAD,
RP COFACTOR, AND DISULFIDE BOND.
RX PubMed=9000629; DOI=10.1006/jmbi.1996.0695;
RA Dai S., Saarinrn M., Ramaswamy S., Meyer Y., Jacquot J.-P., Eklund H.;
RT "Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin
RT reductase at 2.5-A resolution.";
RL J. Mol. Biol. 264:1044-1057(1996).
CC -!- FUNCTION: NADPH-dependent thioredoxin-disulfide reductase that reduces
CC thioredoxins O1, O2 and F3. {ECO:0000269|PubMed:11717467,
CC ECO:0000269|PubMed:8308900}.
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 Evidence={ECO:0000305|PubMed:11717467, ECO:0000305|PubMed:8308900};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347;
CC Evidence={ECO:0000305|PubMed:11717467, ECO:0000305|PubMed:8308900};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:9000629};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:9000629};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 uM for thioredoxin {ECO:0000269|PubMed:8308900};
CC KM=2.2 uM for thioredoxin O1 {ECO:0000269|PubMed:11717467};
CC KM=2.1 uM for thioredoxin O2 {ECO:0000269|PubMed:11717467};
CC KM=3.0 uM for thioredoxin F3 {ECO:0000269|PubMed:11717467};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8308900,
CC ECO:0000269|PubMed:9000629}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11717467,
CC ECO:0000269|PubMed:15642341}. Mitochondrion
CC {ECO:0000269|PubMed:15642341, ECO:0000305|PubMed:25732537}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO42318.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA80656.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=CAB54874.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80262.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z23109; CAA80656.1; ALT_SEQ; mRNA.
DR EMBL; AL117188; CAB54874.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161587; CAB80262.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE86518.1; -; Genomic_DNA.
DR EMBL; BT004322; AAO42318.1; ALT_INIT; mRNA.
DR PIR; S44027; S44027.
DR PIR; T41743; T41743.
DR RefSeq; NP_195271.2; NM_119711.4.
DR PDB; 1VDC; X-ray; 2.50 A; A=43-375.
DR PDBsum; 1VDC; -.
DR AlphaFoldDB; Q39243; -.
DR SMR; Q39243; -.
DR STRING; 3702.AT4G35460.1; -.
DR iPTMnet; Q39243; -.
DR PaxDb; Q39243; -.
DR PRIDE; Q39243; -.
DR ProteomicsDB; 232449; -.
DR EnsemblPlants; AT4G35460.1; AT4G35460.1; AT4G35460.
DR GeneID; 829698; -.
DR Gramene; AT4G35460.1; AT4G35460.1; AT4G35460.
DR KEGG; ath:AT4G35460; -.
DR Araport; AT4G35460; -.
DR TAIR; locus:2117612; AT4G35460.
DR eggNOG; KOG0404; Eukaryota.
DR HOGENOM; CLU_031864_5_1_1; -.
DR InParanoid; Q39243; -.
DR OMA; FRAEDYW; -.
DR OrthoDB; 1108990at2759; -.
DR PhylomeDB; Q39243; -.
DR BioCyc; ARA:AT4G35460-MON; -.
DR BRENDA; 1.8.1.9; 399.
DR EvolutionaryTrace; Q39243; -.
DR PRO; PR:Q39243; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39243; baseline and differential.
DR Genevisible; Q39243; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:TAIR.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0051781; P:positive regulation of cell division; IGI:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Electron transport; FAD;
KW Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Redox-active center;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 38..375
FT /note="Thioredoxin reductase 1, mitochondrial"
FT /id="PRO_0000166771"
FT BINDING 58..61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9000629"
FT BINDING 79..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9000629"
FT BINDING 87..92
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9000629"
FT BINDING 101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9000629"
FT BINDING 134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9000629"
FT BINDING 192
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9000629"
FT BINDING 337
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9000629"
FT BINDING 344..346
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9000629"
FT DISULFID 189..192
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:9000629"
FT CONFLICT 255
FT /note="I -> F (in Ref. 4; AAO42318)"
FT /evidence="ECO:0000305"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:1VDC"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1VDC"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1VDC"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 149..160
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:1VDC"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1VDC"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:1VDC"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1VDC"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:1VDC"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1VDC"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 257..279
FT /evidence="ECO:0007829|PDB:1VDC"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:1VDC"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1VDC"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:1VDC"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1VDC"
FT HELIX 346..366
FT /evidence="ECO:0007829|PDB:1VDC"
SQ SEQUENCE 375 AA; 39626 MW; F86B7FF70340C952 CRC64;
MNCVSRLKCL ISKARSFARL GGESTLSQPP SLASAAFSSS AVMNGLETHN TRLCIVGSGP
AAHTAAIYAA RAELKPLLFE GWMANDIAPG GQLTTTTDVE NFPGFPEGIL GVELTDKFRK
QSERFGTTIF TETVTKVDFS SKPFKLFTDS KAILADAVIL ATGAVAKRLS FVGSGEASGG
FWNRGISACA VCDGAAPIFR NKPLAVIGGG DSAMEEANFL TKYGSKVYII HRRDAFRASK
IMQQRALSNP KIDVIWNSSV VEAYGDGERD VLGGLKVKNV VTGDVSDLKV SGLFFAIGHE
PATKFLDGGV ELDSDGYVVT KPGTTQTSVP GVFAAGDVQD KKYRQAITAA GTGCMAALDA
EHYLQEIGSQ QGKSD
