Reviewed, UniProtKB/Swiss-Prot Q39243 (TRXB1_ARATH)

Names and origin

Protein names

Recommended name:
    Thioredoxin reductase 1
    EC=1.8.1.9
Alternative name(s):
    NADPH-dependent thioredoxin reductase 1
      Short name=NTR 1

Gene names

Name:	NTR1
Ordered Locus Names:	At4g35460
ORF Names:	F15J1.30

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell growth Inferred from genetic interaction. Source: TAIR cell redox homeostasis Inferred from genetic interaction. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pollen germination Inferred from genetic interaction. Source: TAIR removal of superoxide radicals Inferred from electronic annotation. Source: InterPro seed development Inferred from genetic interaction. Source: TAIR thioredoxin biosynthetic process Inferred from genetic interaction. Source: TAIR
Cellular component	chloroplast envelope Inferred from direct assay. Source: TAIR cytosol Inferred from direct assay. Source: TAIR mitochondrion Inferred from direct assay. Source: TAIR
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activity Ref.1 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 333

333

Thioredoxin reductase 1

PRO_0000166771

Amino acid modifications

Disulfide bond

147 ↔ 150

Redox-active Ref.3

Experimental info

Sequence conflict

52 – 57

6

TTTTDV → NQPPR in CAA80656. Ref.1

Sequence conflict

120

1

T → I in CAA80656. Ref.1

Sequence conflict

126

1

R → W in CAA80656. Ref.1

Sequence conflict

135 – 136

2

AS → VL in CAA80656. Ref.1

Sequence conflict

139

1

F → L in CAA80656. Ref.1

Sequence conflict

189

1

H → D in CAA80656. Ref.1

Secondary structure

1

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333

Helix Strand Turn

Details...

Beta strand

5 – 14

10

Helix

18 – 29

12

Beta strand

35 – 37

3

Beta strand

40 – 42

3

Helix

50 – 53

4

Beta strand

55 – 57

3

Helix

69 – 82

14

Beta strand

86 – 88

3

Beta strand

94 – 96

3

Beta strand

98 – 105

8

Beta strand

107 – 118

12

Beta strand

122 – 124

3

Beta strand

133 – 137

5

Turn

141 – 143

3

Beta strand

144 – 146

3

Helix

148 – 151

4

Helix

155 – 157

3

Beta strand

160 – 165

6

Helix

169 – 178

10

Turn

179 – 181

3

Beta strand

182 – 188

7

Beta strand

190 – 193

4

Helix

198 – 205

8

Beta strand

210 – 213

4

Beta strand

215 – 237

23

Turn

238 – 240

3

Beta strand

243 – 247

5

Beta strand

249 – 253

5

Beta strand

257 – 260

4

Helix

262 – 264

3

Beta strand

290 – 292

3

Helix

294 – 297

4

Helix

304 – 324

21

Sequences

	Sequence		Length	Mass (Da)
	Q39243-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: E0056BCCB0DF8794	FASTA	333	35,314
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis thaliana NAPHP thioredoxin reductase. cDNA characterization and expression of the recombinant protein in Escherichia coli." Jacquot J.-P., Rivera-Madrid R., Marinho P., Kollarova M., le Marechal P., Miginiac-Maslow M., Meyer Y. J. Mol. Biol. 235:1357-1363(1994) [PubMed: 8308900] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Silique.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." 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. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5-A resolution." Dai S., Saarinrn M., Ramaswamy S., Meyer Y., Jacquot J.-P., Eklund H. J. Mol. Biol. 264:1044-1057(1996) [PubMed: 9000629] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z23109 mRNA. Translation: CAA80656.1.
AL117188 Genomic DNA. Translation: CAB54874.1.
AL161587 Genomic DNA. Translation: CAB80262.1.

IPI

IPI00548203.

PIR

S44027.
T41743.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VDC	X-ray	2.50	A	1-333	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q39243.

Proteomic databases

PRIDE

Q39243.

Genome annotation databases

GenomeReviews

Gene locus AT4G35460 in contig CT486007_GR.

NMPDR

fig|3702.1.peg.21630.

Organism-specific databases

TAIR

At4g35460.

Phylogenomic databases

eggNOG

KOG0404.

HOGENOM

HBG669726.

InParanoid

Q39243.

PhylomeDB

Q39243.

Enzyme and pathway databases

BRENDA

1.8.1.9. 302.

Gene expression databases

Genevestigator

Q39243.

GermOnline

AT4G35460. Arabidopsis thaliana.

Family and domain databases

InterPro

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_Rdtase.
[Graphical view]

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.
PR00469. PNDRDTASEII.

TIGRFAMs

TIGR01292. TRX_reduct. 1 hit.

PROSITE

PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TRXB1_ARATH

Accession

Primary (citable) accession number: Q39243
Secondary accession number(s): Q9SVW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 1, 2000
Last modified:	February 9, 2010
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)