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Protein

Thioredoxin reductase

Gene

trr1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

  • thioredoxin-disulfide reductase activity Source: PomBase

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)
Alternative name(s):
Caffeine resistance protein 4
Gene namesi
Name:trr1
Synonyms:caf4
ORF Names:SPBC3F6.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC3F6.03.
PomBaseiSPBC3F6.03. trr1.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • mitochondrion Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Thioredoxin reductasePRO_0000166768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi142 ↔ 145Redox-activeBy similarity
Modified residuei192 – 1921Phosphoserine1 Publication
Modified residuei278 – 2781Phosphothreonine1 Publication
Modified residuei279 – 2791Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ92375.
PRIDEiQ92375.

PTM databases

iPTMnetiQ92375.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi280434. 6 interactions.
MINTiMINT-4701472.

Structurei

3D structure databases

ProteinModelPortaliQ92375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000072912.
InParanoidiQ92375.
KOiK00384.
OMAiGQLEMNN.
OrthoDBiEOG7DC2FH.
PhylomeDBiQ92375.

Family and domain databases

Gene3Di3.50.50.60. 3 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.

Q92375-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHNKVVIIG SGPAGHTAAI YLARGELKPV MYEGMLANGI AAGGQLTTTT
60 70 80 90 100
DVENFPGFPD GINGTTLTEN FRAQSLRFGT EIITETVSKL DLSSRPFKYW
110 120 130 140 150
LEGAEEEEPH TADSVILATG ASARRLHITG EDTYWQAGIS ACAVCDGAVP
160 170 180 190 200
IYRNKPLAVV GGGDSAAEEA QFLTKYGSKV YVLVRRDKLR ASPIMAKRLL
210 220 230 240 250
ANPKVEVLWN TVAEEAQGDG KLLNNLRIKN TNTNEVSDLQ VNGLFYAIGH
260 270 280 290 300
IPATKLVAEQ IELDEAGYIK TINGTPRTSI PGFFAAGDVQ DKVFRQAITS
310 320
AGSGCQAALL AMHYLEELED TD
Length:322
Mass (Da):34,618
Last modified:February 1, 1997 - v1
Checksum:i3209D979DA303ECA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63713 Genomic DNA. Translation: AAC49569.1.
AF535134 Genomic DNA. Translation: AAN01228.1.
CU329671 Genomic DNA. Translation: CAA17692.1.
PIRiT40393.
RefSeqiNP_001018848.1. NM_001022668.2.

Genome annotation databases

EnsemblFungiiSPBC3F6.03.1; SPBC3F6.03.1:pep; SPBC3F6.03.
GeneIDi3361358.
KEGGispo:SPBC3F6.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63713 Genomic DNA. Translation: AAC49569.1.
AF535134 Genomic DNA. Translation: AAN01228.1.
CU329671 Genomic DNA. Translation: CAA17692.1.
PIRiT40393.
RefSeqiNP_001018848.1. NM_001022668.2.

3D structure databases

ProteinModelPortaliQ92375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280434. 6 interactions.
MINTiMINT-4701472.

PTM databases

iPTMnetiQ92375.

Proteomic databases

MaxQBiQ92375.
PRIDEiQ92375.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC3F6.03.1; SPBC3F6.03.1:pep; SPBC3F6.03.
GeneIDi3361358.
KEGGispo:SPBC3F6.03.

Organism-specific databases

EuPathDBiFungiDB:SPBC3F6.03.
PomBaseiSPBC3F6.03. trr1.

Phylogenomic databases

HOGENOMiHOG000072912.
InParanoidiQ92375.
KOiK00384.
OMAiGQLEMNN.
OrthoDBiEOG7DC2FH.
PhylomeDBiQ92375.

Miscellaneous databases

PROiQ92375.

Family and domain databases

Gene3Di3.50.50.60. 3 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...

Publicationsi

« Hide 'large scale' publications
  1. "A mutation in a thioredoxin reductase homolog suppresses p53-induced growth inhibition in the fission yeast Schizosaccharomyces pombe."
    Casso D., Beach D.
    Mol. Gen. Genet. 252:518-529(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning of caf1+, caf2+ and caf4+ from Schizosaccharomyces pombe: their involvement in multidrug resistance, UV and pH sensitivity."
    Benko Z., Sipiczki M., Carr A.M.
    Mol. Gen. Genet. 260:434-443(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Molecular characterization and regulation of a gene encoding thioredoxin reductase homolog from the fission Yeast."
    Hong S.-M., Cho Y.-W., Lim C.-J.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; THR-278 AND SER-279, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTRXB_SCHPO
AccessioniPrimary (citable) accession number: Q92375
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 8, 2016
This is version 124 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.