Reviewed, UniProtKB/Swiss-Prot P29509 (TRXB1_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [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.5
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
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from direct assay. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW removal of superoxide radicals Inferred from electronic annotation. Source: InterPro response to oxidative stress Inferred from genetic interaction. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro ferrous iron binding Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct thioredoxin-disulfide reductase activity Ref.1 Inferred from direct assay. 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.6
	Modified residue	94	1	Phosphoserine Ref.6
	Modified residue	193	1	Phosphothreonine Ref.6
	Modified residue	279	1	Phosphoserine Ref.6
	Modified residue	300	1	Phosphoserine Ref.6
	Modified residue	303	1	Phosphoserine Ref.6
	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

Sequences

	Sequence		Length	Mass (Da)
	P29509-1 [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]	"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.
[4]	"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.
[5]	"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].
[6]	"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

EMBLGenBankDDBJ

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

PIR

S61150.

RefSeq

NP_010640.1.

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4319N.

IntAct

P29509. 15 interactions.

Proteomic databases

PeptideAtlas

P29509.

PRIDE

P29509.

Genome annotation databases

Ensembl

YDR353W. Saccharomyces cerevisiae. [Contig view]

GeneID

851955.

GenomeReviews

Gene locus YDR353W in contig Z71256_GR.

KEGG

sce:YDR353W.

NMPDR

fig|4932.3.peg.1406.

Organism-specific databases

CYGD

YDR353w.

SGD

S000002761. TRR1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P29509.

OMA

P29509. YRNREVA.

Enzyme and pathway databases

BRENDA

1.8.1.9. 250.

Gene expression databases

GermOnline

YDR353W. Saccharomyces cerevisiae.

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.

ProDom

PD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01292. TRX_reduct. 1 hit.

PROSITE

PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

970056.

Entry information

Entry name

TRXB1_YEAST

Accession

Primary (citable) accession number: P29509

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)