P29509 (TRXB1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin reductase 1
EC=1.8.1.9

Gene names

Name:	TRR1
Ordered Locus Names:	YDR353W
ORF Names:	D9476.5

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts on thioredoxins 1 and 2.
Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Miscellaneous	The active site is a redox-active disulfide bond. Present with 292000 molecules/cell in log phase SD medium. Ref.6
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 Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from direct assay. Source: SGD removal of superoxide radicals Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: SGD
Molecular function	ferrous iron binding Inferred from direct assay. Source: SGD flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activity Inferred from direct assay Ref.1. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RHO5	P53879	1	EBI-19497,EBI-29054

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 319

318

Thioredoxin reductase 1

PRO_0000166770

Regions

Nucleotide binding

33 – 45

13

FAD By similarity

Nucleotide binding

288 – 297

10

FAD By similarity

Amino acid modifications

Modified residue

11

1

Phosphoserine Ref.7

Modified residue

94

1

Phosphoserine Ref.7

Modified residue

193

1

Phosphothreonine Ref.7

Modified residue

279

1

Phosphoserine Ref.7

Modified residue

300

1

Phosphoserine Ref.7

Modified residue

303

1

Phosphoserine Ref.7

Disulfide bond

142 ↔ 145

Redox-active By similarity

Experimental info

Sequence conflict

18

1

A → V in AAA64747. Ref.1

Sequence conflict

101

1

T → A in AAA64747. Ref.1

Sequence conflict

111

1

T → A in AAA64747. Ref.1

Sequence conflict

180 – 196

17

VFMLV…STIMQ → CLCLSEKTICVLLPLCK in AAA64747. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

319

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Helix

14 – 24

11

Beta strand

30 – 32

3

Helix

46 – 48

3

Helix

66 – 77

12

Beta strand

81 – 83

3

Beta strand

87 – 91

5

Beta strand

93 – 101

9

Beta strand

110 – 117

8

Turn

132 – 136

5

Turn

143 – 145

3

Helix

150 – 152

3

Beta strand

155 – 160

6

Helix

165 – 173

9

Beta strand

179 – 183

5

Beta strand

185 – 188

4

Helix

193 – 201

9

Beta strand

205 – 208

4

Beta strand

210 – 217

8

Beta strand

225 – 230

6

Turn

231 – 234

4

Beta strand

235 – 239

5

Helix

255 – 257

3

Helix

297 – 300

4

Helix

306 – 319

14

Sequences

	Sequence		Length	Mass (Da)
	P29509 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 9F9E58A4BAD859E1	FASTA	319	34,238
	10 20 30 40 50 60 MVHNKVTIIG SGPAAHTAAI YLARAEIKPI LYEGMMANGI AAGGQLTTTT EIENFPGFPD 70 80 90 100 110 120 GLTGSELMDR MREQSTKFGT EIITETVSKV DLSSKPFKLW TEFNEDAEPV TTDAIILATG 130 140 150 160 170 180 ASAKRMHLPG EETYWQKGIS ACAVCDGAVP IFRNKPLAVI GGGDSACEEA QFLTKYGSKV 190 200 210 220 230 240 FMLVRKDHLR ASTIMQKRAE KNEKIEILYN TVALEAKGDG KLLNALRIKN TKKNEETDLP 250 260 270 280 290 300 VSGLFYAIGH TPATKIVAGQ VDTDEAGYIK TVPGSSLTSV PGFFAAGDVQ DSKYRQAITS 310 AGSGCMAALD AEKYLTSLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Thioredoxin-dependent peroxide reductase from yeast." Chae H.Z., Chung S.J., Rhee S.G. J. Biol. Chem. 269:27670-27678(1994) [PubMed: 7961686] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 200358 / YNN 295.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"The TRP4 gene of Saccharomyces cerevisiae: isolation and structural analysis." Furter R., Paravicini G., Aebi M., Braus G., Prantl F., Niederberger P., Huetter R. Nucleic Acids Res. 14:6357-6373(1986) [PubMed: 2428012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-319.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-94; THR-193; SER-279; SER-300 AND SER-303, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U10274 Genomic DNA. Translation: AAA64747.1.
U28372 Genomic DNA. Translation: AAB64789.1.
X04273 Genomic DNA. No translation available.
AY557749 Genomic DNA. Translation: AAS56075.1.
BK006938 Genomic DNA. Translation: DAA12193.1.

PIR

S61150.

RefSeq

NP_010640.1. NM_001180661.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3D8X	X-ray	2.80	A/B	2-319	[»]
3ITJ	X-ray	2.40	A/B/C/D	2-319	[»]

ProteinModelPortal

P29509.

SMR

P29509. Positions 2-319.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4319N.

IntAct

P29509. 12 interactions.

MINT

MINT-488138.

STRING

P29509.

Proteomic databases

PeptideAtlas

P29509.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR353W; YDR353W; YDR353W.

GeneID

851955.

KEGG

sce:YDR353W.

NMPDR

fig|4932.3.peg.1406.

Organism-specific databases

SGD

S000002761. TRR1.

Phylogenomic databases

eggNOG

fuNOG04450.

GeneTree

EFGT00050000005581.

HOGENOM

HBG669726.

OMA

MLEFETI.

OrthoDB

EOG4HB1V7.

Gene expression databases

ArrayExpress

P29509.

Genevestigator

P29509.

GermOnline

YDR353W. Saccharomyces cerevisiae.

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...

Other

NextBio

970056.

Entry information

Entry name

TRXB1_YEAST

Accession

Primary (citable) accession number: P29509
Secondary accession number(s): D6VSY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program