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Protein

Thioredoxin reductase 2, mitochondrial

Gene

TRR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts on mitochondrial thioredoxin 3. Implicated in the defense against oxidative stress.

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 6813FADBy similarityAdd
BLAST
Nucleotide bindingi311 – 32010FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. thioredoxin-disulfide reductase activity Source: SGD

GO - Biological processi

  1. cell redox homeostasis Source: SGD
  2. cellular response to oxidative stress Source: SGD
  3. removal of superoxide radicals Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciYEAST:YHR106W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 2, mitochondrial (EC:1.8.1.9)
Gene namesi
Name:TRR2
Ordered Locus Names:YHR106W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

CYGDiYHR106w.
SGDiS000001148. TRR2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionSequence AnalysisAdd
BLAST
Chaini24 – 342319Thioredoxin reductase 2, mitochondrialPRO_0000030303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi165 ↔ 168Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP38816.
PaxDbiP38816.
PeptideAtlasiP38816.

Expressioni

Gene expression databases

GenevestigatoriP38816.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi36539. 26 interactions.
DIPiDIP-1942N.
IntActiP38816. 2 interactions.
MINTiMINT-396494.
STRINGi4932.YHR106W.

Structurei

3D structure databases

ProteinModelPortaliP38816.
SMRiP38816. Positions 25-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG0492.
GeneTreeiENSGT00390000011774.
HOGENOMiHOG000072912.
InParanoidiP38816.
KOiK00384.
OMAiHQLDYFQ.
OrthoDBiEOG7DC2FH.

Family and domain databases

InterProiIPR013027. 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]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
PR00469. PNDRDTASEII.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38816-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKHIVSPFR TNFVGISKSV LSRMIHHKVT IIGSGPAAHT AAIYLARAEM
60 70 80 90 100
KPTLYEGMMA NGIAAGGQLT TTTDIENFPG FPESLSGSEL MERMRKQSAK
110 120 130 140 150
FGTNIITETV SKVDLSSKPF RLWTEFNEDA EPVTTDAIIL ATGASAKRMH
160 170 180 190 200
LPGEETYWQQ GISACAVCDG AVPIFRNKPL AVIGGGDSAC EEAEFLTKYA
210 220 230 240 250
SKVYILVRKD HFRASVIMQR RIEKNPNIIV LFNTVALEAK GDGKLLNMLR
260 270 280 290 300
IKNTKSNVEN DLEVNGLFYA IGHSPATDIV KGQVDEEETG YIKTVPGSSL
310 320 330 340
TSVPGFFAAG DVQDSRYRQA VTSAGSGCIA ALDAERYLSA QE
Length:342
Mass (Da):37,087
Last modified:February 1, 1995 - v1
Checksum:i739F302AA0837A5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00059 Genomic DNA. Translation: AAB68856.1.
AY557882 Genomic DNA. Translation: AAS56208.1.
BK006934 Genomic DNA. Translation: DAA06800.1.
PIRiS48948.
RefSeqiNP_011974.1. NM_001179236.1.

Genome annotation databases

EnsemblFungiiYHR106W; YHR106W; YHR106W.
GeneIDi856506.
KEGGisce:YHR106W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00059 Genomic DNA. Translation: AAB68856.1.
AY557882 Genomic DNA. Translation: AAS56208.1.
BK006934 Genomic DNA. Translation: DAA06800.1.
PIRiS48948.
RefSeqiNP_011974.1. NM_001179236.1.

3D structure databases

ProteinModelPortaliP38816.
SMRiP38816. Positions 25-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36539. 26 interactions.
DIPiDIP-1942N.
IntActiP38816. 2 interactions.
MINTiMINT-396494.
STRINGi4932.YHR106W.

Proteomic databases

MaxQBiP38816.
PaxDbiP38816.
PeptideAtlasiP38816.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR106W; YHR106W; YHR106W.
GeneIDi856506.
KEGGisce:YHR106W.

Organism-specific databases

CYGDiYHR106w.
SGDiS000001148. TRR2.

Phylogenomic databases

eggNOGiCOG0492.
GeneTreeiENSGT00390000011774.
HOGENOMiHOG000072912.
InParanoidiP38816.
KOiK00384.
OMAiHQLDYFQ.
OrthoDBiEOG7DC2FH.

Enzyme and pathway databases

BioCyciYEAST:YHR106W-MONOMER.

Miscellaneous databases

NextBioi982236.

Gene expression databases

GenevestigatoriP38816.

Family and domain databases

InterProiIPR013027. 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]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
PR00469. PNDRDTASEII.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae."
    Pedrajas J.R., Kosmidou E., Miranda-Vizuete A., Gustafsson J.-A., Wright A.P.H., Spyrou G.
    J. Biol. Chem. 274:6366-6373(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRXB2_YEAST
AccessioniPrimary (citable) accession number: P38816
Secondary accession number(s): D3DL56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 414 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.