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P29509

- TRXB1_YEAST

UniProt

P29509 - TRXB1_YEAST

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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

Functioni

Acts on thioredoxins 1 and 2.

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADBy similarityNote: 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
Complete GO annotation...

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
Complete GO annotation...

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. 42 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 – 97Combined sources
Helixi13 – 2412Combined sources
Beta strandi30 – 323Combined sources
Beta strandi35 – 373Combined sources
Helixi45 – 484Combined sources
Beta strandi49 – 524Combined sources
Helixi64 – 7714Combined sources
Beta strandi81 – 833Combined sources
Beta strandi87 – 915Combined sources
Beta strandi93 – 1019Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi110 – 1178Combined sources
Beta strandi121 – 1233Combined sources
Helixi131 – 1344Combined sources
Turni136 – 1383Combined sources
Beta strandi139 – 1413Combined sources
Helixi143 – 1464Combined sources
Helixi150 – 1523Combined sources
Beta strandi155 – 1606Combined sources
Helixi164 – 17310Combined sources
Turni174 – 1763Combined sources
Beta strandi177 – 1837Combined sources
Beta strandi185 – 1884Combined sources
Helixi193 – 2019Combined sources
Beta strandi205 – 2084Combined sources
Beta strandi210 – 23021Combined sources
Turni231 – 2344Combined sources
Beta strandi235 – 2406Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi250 – 2523Combined sources
Helixi255 – 2573Combined sources
Turni258 – 2603Combined sources
Beta strandi275 – 2773Combined sources
Beta strandi283 – 2853Combined sources
Helixi287 – 2904Combined sources
Helixi297 – 31519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP29509.
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

        10         20         30         40         50
MVHNKVTIIG SGPAAHTAAI YLARAEIKPI LYEGMMANGI AAGGQLTTTT
60 70 80 90 100
EIENFPGFPD GLTGSELMDR MREQSTKFGT EIITETVSKV DLSSKPFKLW
110 120 130 140 150
TEFNEDAEPV TTDAIILATG ASAKRMHLPG EETYWQKGIS ACAVCDGAVP
160 170 180 190 200
IFRNKPLAVI GGGDSACEEA QFLTKYGSKV FMLVRKDHLR ASTIMQKRAE
210 220 230 240 250
KNEKIEILYN TVALEAKGDG KLLNALRIKN TKKNEETDLP VSGLFYAIGH
260 270 280 290 300
TPATKIVAGQ VDTDEAGYIK TVPGSSLTSV PGFFAAGDVQ DSKYRQAITS
310
AGSGCMAALD AEKYLTSLE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 42 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.
InParanoidi P29509.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 147 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