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Protein

Thioredoxin reductase 1

Gene

TRR1

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

Functioni

Acts on thioredoxins 1 and 2.1 Publication

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei45FAD; via amide nitrogen2 Publications1
Binding sitei54FAD2 Publications1
Binding sitei87FAD; via amide nitrogen and carbonyl oxygen2 Publications1
Binding sitei145FAD2 Publications1
Binding sitei288FAD2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 14FAD2 Publications4
Nucleotide bindingi40 – 41FAD2 Publications2
Nucleotide bindingi295 – 297FAD2 Publications3

GO - Molecular functioni

  • ferrous iron binding Source: SGD
  • thioredoxin-disulfide reductase activity Source: SGD

GO - Biological processi

  • cell redox homeostasis Source: SGD
  • cellular response to oxidative stress Source: SGD
  • 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.
BRENDAi1.8.1.9. 984.

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
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR353W.
SGDiS000002761. TRR1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • mitochondrial intermembrane space Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001667702 – 319Thioredoxin reductase 1Add BLAST318

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi142 ↔ 145Redox-active1 Publication
Modified residuei303PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP29509.
PRIDEiP29509.

PTM databases

iPTMnetiP29509.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi32410. 41 interactors.
DIPiDIP-4319N.
IntActiP29509. 4 interactors.
MINTiMINT-488138.

Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi13 – 24Combined sources12
Beta strandi30 – 32Combined sources3
Beta strandi35 – 37Combined sources3
Helixi45 – 48Combined sources4
Beta strandi49 – 52Combined sources4
Helixi64 – 77Combined sources14
Beta strandi81 – 83Combined sources3
Beta strandi87 – 91Combined sources5
Beta strandi93 – 101Combined sources9
Beta strandi105 – 107Combined sources3
Beta strandi110 – 117Combined sources8
Beta strandi121 – 123Combined sources3
Helixi131 – 134Combined sources4
Turni136 – 138Combined sources3
Beta strandi139 – 141Combined sources3
Helixi143 – 146Combined sources4
Helixi150 – 152Combined sources3
Beta strandi155 – 160Combined sources6
Helixi164 – 173Combined sources10
Turni174 – 176Combined sources3
Beta strandi177 – 183Combined sources7
Beta strandi185 – 188Combined sources4
Helixi193 – 201Combined sources9
Beta strandi205 – 208Combined sources4
Beta strandi210 – 230Combined sources21
Turni231 – 234Combined sources4
Beta strandi235 – 240Combined sources6
Beta strandi242 – 246Combined sources5
Beta strandi250 – 252Combined sources3
Helixi255 – 257Combined sources3
Turni258 – 260Combined sources3
Beta strandi275 – 277Combined sources3
Beta strandi283 – 285Combined sources3
Helixi287 – 290Combined sources4
Helixi297 – 315Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3D8XX-ray2.80A/B2-319[»]
3ITJX-ray2.40A/B/C/D2-319[»]
ProteinModelPortaliP29509.
SMRiP29509.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29509.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00390000011774.
HOGENOMiHOG000072912.
InParanoidiP29509.
KOiK00384.
OMAiKQEDNSM.
OrthoDBiEOG092C3AEY.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti18A → V in AAA64747 (PubMed:7961686).Curated1
Sequence conflicti101T → A in AAA64747 (PubMed:7961686).Curated1
Sequence conflicti111T → A in AAA64747 (PubMed:7961686).Curated1
Sequence conflicti180 – 196VFMLV…STIMQ → CLCLSEKTICVLLPLCK in AAA64747 (PubMed:7961686).CuratedAdd BLAST17

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.
PIRiS61150.
RefSeqiNP_010640.1. NM_001180661.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3D8XX-ray2.80A/B2-319[»]
3ITJX-ray2.40A/B/C/D2-319[»]
ProteinModelPortaliP29509.
SMRiP29509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32410. 41 interactors.
DIPiDIP-4319N.
IntActiP29509. 4 interactors.
MINTiMINT-488138.

PTM databases

iPTMnetiP29509.

Proteomic databases

MaxQBiP29509.
PRIDEiP29509.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YDR353W.
SGDiS000002761. TRR1.

Phylogenomic databases

GeneTreeiENSGT00390000011774.
HOGENOMiHOG000072912.
InParanoidiP29509.
KOiK00384.
OMAiKQEDNSM.
OrthoDBiEOG092C3AEY.

Enzyme and pathway databases

BioCyciYEAST:YDR353W-MONOMER.
BRENDAi1.8.1.9. 984.

Miscellaneous databases

EvolutionaryTraceiP29509.
PROiP29509.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 162 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

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 one 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.