Q39243 (TRXB1_ARATH) Reviewed, UniProtKB/Swiss-Prot

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=NTR1
NADPH-dependent thioredoxin reductase B
Short name=AtNTRB

Gene names

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

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Possesses thioredoxin-disulfide reductase activity towards thioredoxins O1, O2 and F3. Ref.5
Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm. Mitochondrion Ref.5 Ref.6.
Tissue specificity	Ubiquitous.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Sequence caution	The sequence AAO42318.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAA80656.1 differs from that shown. Reason: Sequencing errors. The sequence CAB54874.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAB80262.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm Mitochondrion
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell growth Inferred from genetic interaction. Source: TAIR cell redox homeostasis Inferred from genetic interaction. Source: TAIR electron transport chain 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 transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast envelope Inferred from direct assay. Source: TAIR cytosol Inferred from direct assay Ref.6. Source: TAIR mitochondrion Inferred from direct assay Ref.6. Source: TAIR
Molecular function	flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activity Inferred from direct assay Ref.5Ref.3. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 375

375

Thioredoxin reductase 1

PRO_0000166771

Regions

Nucleotide binding

58 – 61

4

FAD

Nucleotide binding

79 – 80

2

FAD

Nucleotide binding

87 – 92

6

FAD

Nucleotide binding

344 – 346

3

FAD

Sites

Binding site

101

1

FAD

Binding site

134

1

FAD; via amide nitrogen and carbonyl oxygen

Binding site

192

1

FAD

Binding site

337

1

FAD

Amino acid modifications

Disulfide bond

189 ↔ 192

Redox-active Ref.7

Experimental info

Sequence conflict

255

1

I → F in AAO42318. Ref.4

Secondary structure

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375

Helix Strand Turn

Details...

Beta strand

47 – 56

10

Helix

60 – 71

12

Beta strand

77 – 79

3

Beta strand

82 – 84

3

Helix

92 – 95

4

Beta strand

97 – 99

3

Helix

111 – 124

14

Beta strand

128 – 130

3

Beta strand

136 – 138

3

Beta strand

140 – 147

8

Beta strand

149 – 160

12

Beta strand

164 – 166

3

Beta strand

175 – 179

5

Turn

183 – 185

3

Beta strand

186 – 188

3

Helix

190 – 193

4

Helix

197 – 199

3

Beta strand

202 – 207

6

Helix

211 – 220

10

Turn

221 – 223

3

Beta strand

224 – 230

7

Beta strand

232 – 235

4

Helix

240 – 247

8

Beta strand

252 – 255

4

Beta strand

257 – 279

23

Turn

280 – 282

3

Beta strand

285 – 289

5

Beta strand

291 – 295

5

Beta strand

299 – 302

4

Helix

304 – 306

3

Beta strand

332 – 334

3

Helix

336 – 339

4

Helix

346 – 366

21

Sequences

	Sequence		Length	Mass (Da)
	Q39243 [UniParc]. Last modified June 15, 2010. Version 3. Checksum: F86B7FF70340C952	FASTA	375	39,626
	10 20 30 40 50 60 MNCVSRLKCL ISKARSFARL GGESTLSQPP SLASAAFSSS AVMNGLETHN TRLCIVGSGP 70 80 90 100 110 120 AAHTAAIYAA RAELKPLLFE GWMANDIAPG GQLTTTTDVE NFPGFPEGIL GVELTDKFRK 130 140 150 160 170 180 QSERFGTTIF TETVTKVDFS SKPFKLFTDS KAILADAVIL ATGAVAKRLS FVGSGEASGG 190 200 210 220 230 240 FWNRGISACA VCDGAAPIFR NKPLAVIGGG DSAMEEANFL TKYGSKVYII HRRDAFRASK 250 260 270 280 290 300 IMQQRALSNP KIDVIWNSSV VEAYGDGERD VLGGLKVKNV VTGDVSDLKV SGLFFAIGHE 310 320 330 340 350 360 PATKFLDGGV ELDSDGYVVT KPGTTQTSVP GVFAAGDVQD KKYRQAITAA GTGCMAALDA 370 EHYLQEIGSQ QGKSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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] OF 12-375. Tissue: Silique.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-375. Strain: cv. Columbia.
[5]	"Identification and characterization of a mitochondrial thioredoxin system in plants." Laloi C., Rayapuram N., Chartier Y., Grienenberger J.M., Bonnard G., Meyer Y. Proc. Natl. Acad. Sci. U.S.A. 98:14144-14149(2001) [PubMed: 11717467] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana." Reichheld J.P., Meyer E., Khafif M., Bonnard G., Meyer Y. FEBS Lett. 579:337-342(2005) [PubMed: 15642341] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"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) OF 43-375 IN COMPLEX WITH FAD, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z23109 mRNA. Translation: CAA80656.1. Sequence problems.
AL117188 Genomic DNA. Translation: CAB54874.1. Different initiation.
AL161587 Genomic DNA. Translation: CAB80262.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE86518.1.
BT004322 mRNA. Translation: AAO42318.1. Different initiation.

IPI

IPI00548203.

PIR

S44027.
T41743.

RefSeq

NP_195271.2. NM_119711.3.

UniGene

At.3705.
At.69236.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VDC	X-ray	2.50	A	43-375	[»]

ProteinModelPortal

Q39243.

SMR

Q39243. Positions 46-367.

ModBase

Search...

Protein-protein interaction databases

STRING

Q39243.

Proteomic databases

PRIDE

Q39243.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT4G35460.1; AT4G35460.1; AT4G35460.

GeneID

829698.

GenomeReviews

Gene locus AT4G35460 in contig CT486007_GR.

KEGG

ath:AT4G35460.

NMPDR

fig|3702.1.peg.21630.

Organism-specific databases

TAIR

At4g35460.

Phylogenomic databases

eggNOG

KOG0404.

GeneTree

EPGT00070000029765.

HOGENOM

HBG669726.

InParanoid

Q39243.

OMA

MREHAER.

PhylomeDB

Q39243.

ProtClustDB

CLSN2688871.

Enzyme and pathway databases

BioCyc

ARA:AT4G35460-MONOMER.

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.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]

KO

K00384.

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): Q84W20, Q9SVW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	June 15, 2010
Last modified:	November 16, 2011
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program