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P38816

- TRXB2_YEAST

UniProt

P38816 - TRXB2_YEAST

Protein

Thioredoxin reductase 2, mitochondrial

Gene

TRR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

    Cofactori

    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

    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

    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. 24 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.
    KOiK00384.
    OMAiMANIASK.
    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

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    MIKHIVSPFR TNFVGISKSV LSRMIHHKVT IIGSGPAAHT AAIYLARAEM    50
    KPTLYEGMMA NGIAAGGQLT TTTDIENFPG FPESLSGSEL MERMRKQSAK 100
    FGTNIITETV SKVDLSSKPF RLWTEFNEDA EPVTTDAIIL ATGASAKRMH 150
    LPGEETYWQQ GISACAVCDG AVPIFRNKPL AVIGGGDSAC EEAEFLTKYA 200
    SKVYILVRKD HFRASVIMQR RIEKNPNIIV LFNTVALEAK GDGKLLNMLR 250
    IKNTKSNVEN DLEVNGLFYA IGHSPATDIV KGQVDEEETG YIKTVPGSSL 300
    TSVPGFFAAG DVQDSRYRQA VTSAGSGCIA ALDAERYLSA QE 342
    Length:342
    Mass (Da):37,087
    Last modified:February 1, 1995 - v1
    Checksum:i739F302AA0837A5A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00059 Genomic DNA. Translation: AAB68856.1 .
    AY557882 Genomic DNA. Translation: AAS56208.1 .
    BK006934 Genomic DNA. Translation: DAA06800.1 .
    PIRi S48948.
    RefSeqi NP_011974.1. NM_001179236.1.

    3D structure databases

    ProteinModelPortali P38816.
    SMRi P38816. Positions 25-342.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36539. 24 interactions.
    DIPi DIP-1942N.
    IntActi P38816. 2 interactions.
    MINTi MINT-396494.
    STRINGi 4932.YHR106W.

    Proteomic databases

    MaxQBi P38816.
    PaxDbi P38816.
    PeptideAtlasi P38816.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YHR106W ; YHR106W ; YHR106W .
    GeneIDi 856506.
    KEGGi sce:YHR106W.

    Organism-specific databases

    CYGDi YHR106w.
    SGDi S000001148. TRR2.

    Phylogenomic databases

    eggNOGi COG0492.
    GeneTreei ENSGT00390000011774.
    HOGENOMi HOG000072912.
    KOi K00384.
    OMAi MANIASK.
    OrthoDBi EOG7DC2FH.

    Enzyme and pathway databases

    BioCyci YEAST:YHR106W-MONOMER.

    Miscellaneous databases

    NextBioi 982236.

    Gene expression databases

    Genevestigatori P38816.

    Family and domain databases

    InterProi 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 ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    PR00469. PNDRDTASEII.
    TIGRFAMsi TIGR01292. TRX_reduct. 1 hit.
    PROSITEi PS00573. PYRIDINE_REDOX_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 128 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