ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q39243


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TRXB1_ARATH
Primary accession number Q39243
Secondary accession number Q9SVW9
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 80)
Name and origin of the protein
Protein name Thioredoxin reductase 1
Synonyms EC 1.8.1.9
NADPH-dependent thioredoxin reductase 1
NTR 1
Gene name
Name: NTR1
OrderedLocusNames: At4g35460
ORFNames: F15J1.30
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Silique;
DOI=10.1006/jmbi.1994.1091; PubMed=8308900 [NCBI, ExPASy, EBI, Israel, Japan]
Jacquot J.-P., Rivera-Madrid R., Marinho P., Kollarova M., le Marechal P., Miginiac-Maslow M., Meyer Y.;
"Arabidopsis thaliana NAPHP thioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli.";
J. Mol. Biol. 235:1357-1363(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND DISULFIDE BOND.
DOI=10.1006/jmbi.1996.0695; PubMed=9000629 [NCBI, ExPASy, EBI, Israel, Japan]
Dai S., Saarinrn M., Ramaswamy S., Meyer Y., Jacquot J.-P., Eklund H.;
"Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5-A resolution.";
J. Mol. Biol. 264:1044-1057(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z23109; CAA80656.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL117188; CAB54874.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161587; CAB80262.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S44027; S44027.
T41743; T41743.
3D structure databases
PDB
1VDC; X-ray; 2.50 A; A=1-333.[ExPASy / RCSB / EBI]
PDBsum 1VDC; -.
ModBase Q39243.
Organism-specific databases
TAIR At4g35460; -.
Gene expression databases
GermOnline AT4G35460; Arabidopsis thaliana.
Ontologies
GO
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000759; Adrndx_reductase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
IPR005982; Thioredox_reduct.
Graphical view of domain structure.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01292; TRX_reduct; 1.
PROSITE PS00573; PYRIDINE_REDOX_2; 1.
BLOCKS Q39243.
ProtoNet Q39243.
Genome annotation databases
GenomeReviews CT486007_GR; AT4G35460.
NMPDR fig|3702.1.peg.21630; -.
Other
LinkHub Q39243; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   333  333     Thioredoxin reductase 1. PRO_0000166771
DISULFID   147   150        Redox-active. 
CONFLICT   52    57        TTTTDV -> NQPPR (in Ref. 1; CAA80656). 
CONFLICT   120   120        T -> I (in Ref. 1; CAA80656). 
CONFLICT   126   126        R -> W (in Ref. 1; CAA80656). 
CONFLICT   135   136        AS -> VL (in Ref. 1; CAA80656). 
CONFLICT   139   139        F -> L (in Ref. 1; CAA80656). 
CONFLICT   189   189        H -> D (in Ref. 1; CAA80656). 
STRAND   5    14  10      
HELIX   18    29  12      
STRAND   35    37  3      
STRAND   40    42  3      
HELIX   50    53  4      
STRAND   55    57  3      
HELIX   69    82  14      
STRAND   86    88  3      
STRAND   94    96  3      
STRAND   98   105  8      
STRAND   107   118  12      
STRAND   122   124  3      
STRAND   133   137  5      
TURN   141   143  3      
STRAND   144   146  3      
HELIX   148   151  4      
HELIX   155   157  3      
STRAND   160   165  6      
HELIX   169   178  10      
TURN   179   181  3      
STRAND   182   188  7      
STRAND   190   193  4      
HELIX   198   205  8      
STRAND   210   213  4      
STRAND   215   237  23      
TURN   238   240  3      
STRAND   243   247  5      
STRAND   249   253  5      
STRAND   257   260  4      
HELIX   262   264  3      
STRAND   290   292  3      
HELIX   294   297  4      
HELIX   304   324  21      
Sequence information
Length: 333 AA [This is the length of the unprocessed precursor] Molecular weight: 35314 Da [This is the MW of the unprocessed precursor] CRC64: E0056BCCB0DF8794 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNGLETHNTR LCIVGSGPAA HTAAIYAARA ELKPLLFEGW MANDIAPGGQ LTTTTDVENF 

        70         80         90        100        110        120 
PGFPEGILGV ELTDKFRKQS ERFGTTIFTE TVTKVDFSSK PFKLFTDSKA ILADAVILAT 

       130        140        150        160        170        180 
GAVAKRLSFV GSGEASGGFW NRGISACAVC DGAAPIFRNK PLAVIGGGDS AMEEANFLTK 

       190        200        210        220        230        240 
YGSKVYIIHR RDAFRASKIM QQRALSNPKI DVIWNSSVVE AYGDGERDVL GGLKVKNVVT 

       250        260        270        280        290        300 
GDVSDLKVSG LFFAIGHEPA TKFLDGGVEL DSDGYVVTKP GTTQTSVPGV FAAGDVQDKK 

       310        320        330 
YRQAITAAGT GCMAALDAEH YLQEIGSQQG KSD 

Q39243 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!