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P29509

- TRXB1_YEAST

UniProt

P29509 - TRXB1_YEAST

Protein

Thioredoxin reductase 1

Gene

TRR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Acts on thioredoxins 1 and 2.

    Catalytic activityi

    Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei45 – 451FAD; via amide nitrogen2 Publications
    Binding sitei54 – 541FAD2 Publications
    Binding sitei87 – 871FAD; via amide nitrogen and carbonyl oxygen2 Publications
    Binding sitei145 – 1451FAD2 Publications
    Binding sitei288 – 2881FAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 144FAD2 Publications
    Nucleotide bindingi40 – 412FAD2 Publications
    Nucleotide bindingi295 – 2973FAD2 Publications

    GO - Molecular functioni

    1. ferrous iron binding Source: SGD
    2. flavin adenine dinucleotide binding Source: InterPro
    3. 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:YDR353W-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin reductase 1 (EC:1.8.1.9)
    Gene namesi
    Name:TRR1
    Ordered Locus Names:YDR353W
    ORF Names:D9476.5
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    SGDiS000002761. TRR1.

    Subcellular locationi

    Cytoplasm 1 Publication. Mitochondrion intermembrane space 1 Publication

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. mitochondrial intermembrane space Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 319318Thioredoxin reductase 1PRO_0000166770Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi142 ↔ 145Redox-active
    Modified residuei303 – 3031Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP29509.
    PaxDbiP29509.
    PeptideAtlasiP29509.
    PRIDEiP29509.

    Expressioni

    Gene expression databases

    GenevestigatoriP29509.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi32410. 41 interactions.
    DIPiDIP-4319N.
    IntActiP29509. 4 interactions.
    MINTiMINT-488138.
    STRINGi4932.YDR353W.

    Structurei

    Secondary structure

    1
    319
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 97
    Helixi13 – 2412
    Beta strandi30 – 323
    Beta strandi35 – 373
    Helixi45 – 484
    Beta strandi49 – 524
    Helixi64 – 7714
    Beta strandi81 – 833
    Beta strandi87 – 915
    Beta strandi93 – 1019
    Beta strandi105 – 1073
    Beta strandi110 – 1178
    Beta strandi121 – 1233
    Helixi131 – 1344
    Turni136 – 1383
    Beta strandi139 – 1413
    Helixi143 – 1464
    Helixi150 – 1523
    Beta strandi155 – 1606
    Helixi164 – 17310
    Turni174 – 1763
    Beta strandi177 – 1837
    Beta strandi185 – 1884
    Helixi193 – 2019
    Beta strandi205 – 2084
    Beta strandi210 – 23021
    Turni231 – 2344
    Beta strandi235 – 2406
    Beta strandi242 – 2465
    Beta strandi250 – 2523
    Helixi255 – 2573
    Turni258 – 2603
    Beta strandi275 – 2773
    Beta strandi283 – 2853
    Helixi287 – 2904
    Helixi297 – 31519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3D8XX-ray2.80A/B2-319[»]
    3ITJX-ray2.40A/B/C/D2-319[»]
    ProteinModelPortaliP29509.
    SMRiP29509. Positions 2-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29509.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0492.
    GeneTreeiENSGT00390000011774.
    HOGENOMiHOG000072912.
    KOiK00384.
    OMAiQTETHVP.
    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.

    P29509-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVHNKVTIIG SGPAAHTAAI YLARAEIKPI LYEGMMANGI AAGGQLTTTT    50
    EIENFPGFPD GLTGSELMDR MREQSTKFGT EIITETVSKV DLSSKPFKLW 100
    TEFNEDAEPV TTDAIILATG ASAKRMHLPG EETYWQKGIS ACAVCDGAVP 150
    IFRNKPLAVI GGGDSACEEA QFLTKYGSKV FMLVRKDHLR ASTIMQKRAE 200
    KNEKIEILYN TVALEAKGDG KLLNALRIKN TKKNEETDLP VSGLFYAIGH 250
    TPATKIVAGQ VDTDEAGYIK TVPGSSLTSV PGFFAAGDVQ DSKYRQAITS 300
    AGSGCMAALD AEKYLTSLE 319
    Length:319
    Mass (Da):34,238
    Last modified:January 23, 2007 - v3
    Checksum:i9F9E58A4BAD859E1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181A → V in AAA64747. (PubMed:7961686)Curated
    Sequence conflicti101 – 1011T → A in AAA64747. (PubMed:7961686)Curated
    Sequence conflicti111 – 1111T → A in AAA64747. (PubMed:7961686)Curated
    Sequence conflicti180 – 19617VFMLV…STIMQ → CLCLSEKTICVLLPLCK in AAA64747. (PubMed:7961686)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS61150.
    RefSeqiNP_010640.1. NM_001180661.1.

    Genome annotation databases

    EnsemblFungiiYDR353W; YDR353W; YDR353W.
    GeneIDi851955.
    KEGGisce:YDR353W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S61150.
    RefSeqi NP_010640.1. NM_001180661.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P29509.
    SMRi P29509. Positions 2-319.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32410. 41 interactions.
    DIPi DIP-4319N.
    IntActi P29509. 4 interactions.
    MINTi MINT-488138.
    STRINGi 4932.YDR353W.

    Proteomic databases

    MaxQBi P29509.
    PaxDbi P29509.
    PeptideAtlasi P29509.
    PRIDEi P29509.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR353W ; YDR353W ; YDR353W .
    GeneIDi 851955.
    KEGGi sce:YDR353W.

    Organism-specific databases

    SGDi S000002761. TRR1.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci YEAST:YDR353W-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P29509.
    NextBioi 970056.

    Gene expression databases

    Genevestigatori P29509.

    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. "Thioredoxin-dependent peroxide reductase from yeast."
      Chae H.Z., Chung S.J., Rhee S.G.
      J. Biol. Chem. 269:27670-27678(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE OF 2-16; 90-97; 126-137; 176-179; 233-238 AND 296-303, CLEAVAGE OF INITIATOR METHIONINE.
      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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-319.
    6. 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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Crystal structure of Saccharomyces cerevisiae cytoplasmic thioredoxin reductase Trr1 reveals the structural basis for species-specific recognition of thioredoxin."
      Zhang Z., Bao R., Zhang Y., Yu J., Zhou C.Z., Chen Y.
      Biochim. Biophys. Acta 1794:124-128(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-319 IN COMPLEX WITH FAD.
    10. "Insights into the specificity of thioredoxin reductase-thioredoxin interactions. A structural and functional investigation of the yeast thioredoxin system."
      Oliveira M.A., Discola K.F., Alves S.V., Medrano F.J., Guimaraes B.G., Netto L.E.
      Biochemistry 49:3317-3326(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-319 IN COMPLEX WITH FAD.

    Entry informationi

    Entry nameiTRXB1_YEAST
    AccessioniPrimary (citable) accession number: P29509
    Secondary accession number(s): D6VSY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.
    Present with 292000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3