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Protein

Thioredoxin reductase

Gene

TRR1

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 nitrogenBy similarity
Binding sitei54 – 541FADBy similarity
Binding sitei87 – 871FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei145 – 1451FADBy similarity
Binding sitei288 – 2881FADBy similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase (EC:1.8.1.9)
Gene namesi
Name:TRR1
Ordered Locus Names:YALI0D27126g
OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic identifieri284591 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
Proteomesi
  • UP000001300 Componenti: Chromosome D

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319Thioredoxin reductasePRO_0000166769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi142 ↔ 145Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ6C7L4.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6C7L4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000072912.
InParanoidiQ6C7L4.
KOiK00384.
OMAiGQLEMNN.
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.

Q6C7L4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHSPVVIIG SGPAAHTAAI YLSRAEIKPT LYEGMMANGI AAGGQLTTTT
60 70 80 90 100
EIENFPGFPD GIMGSQLMED MRKQSIRFGT EIITETVSKV DLSQRPFKYW
110 120 130 140 150
TEFNEDEEPH TADAIILATG ASAKRLSLPG EDQYWQQGIS ACAVCDGAVP
160 170 180 190 200
IFRNKPLAVV GGGDSAAEEA LFLTKYGSKV YVIVRKDKLR ASAVMAKRLA
210 220 230 240 250
SHPKVEILFN HVSIEAKGDG KLLNALEIEN TLTGEKRDLE VNGLFYAIGH
260 270 280 290 300
IPATSIVKGQ VETDEEGYVV TVPGTANTSV KGVFAAGDVQ DKRYRQAITS
310
AGTGCMAALD CEKLLAEEE
Length:319
Mass (Da):34,244
Last modified:August 16, 2004 - v1
Checksum:iE6A192847B409318
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382130 Genomic DNA. Translation: CAG81554.1.
RefSeqiXP_503348.1. XM_503348.1.

Genome annotation databases

EnsemblFungiiCAG81554; CAG81554; YALI0_D27126g.
GeneIDi2911244.
KEGGiyli:YALI0D27126g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382130 Genomic DNA. Translation: CAG81554.1.
RefSeqiXP_503348.1. XM_503348.1.

3D structure databases

ProteinModelPortaliQ6C7L4.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ6C7L4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG81554; CAG81554; YALI0_D27126g.
GeneIDi2911244.
KEGGiyli:YALI0D27126g.

Phylogenomic databases

HOGENOMiHOG000072912.
InParanoidiQ6C7L4.
KOiK00384.
OMAiGQLEMNN.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiTRXB_YARLI
AccessioniPrimary (citable) accession number: Q6C7L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: August 16, 2004
Last modified: September 7, 2016
This is version 78 of the entry and version 1 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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.