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Reviewed, UniProtKB/Swiss-Prot Q75CM8 (TRXB_ASHGO)

Last modified June 16, 2009. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Thioredoxin reductase
    EC=1.8.1.9
Gene names
Name: TRR1
Ordered Locus Names: ACL109C
OrganismAshbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier33169 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

removal of superoxide radicals

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

thioredoxin-disulfide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Thioredoxin reductase
PRO_0000166761

Regions

Nucleotide binding33 – 4513FAD By similarity
Nucleotide binding288 – 29710FAD By similarity

Amino acid modifications

Disulfide bond142 ↔ 145Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q75CM8-1 [UniParc].

Last modified November 9, 2004. Version 2.
Checksum: F7151B685B7802FC

FASTA31934,117
        10         20         30         40         50         60 
MVHHKVTIIG SGPAAHTAAI YLARAEIKPT LYEGMFANGV AAGGQLTTTT EIENFPGFPD 

        70         80         90        100        110        120 
GLTGSDLMER MKAQSVKFGT EVVTETVAKV DLSARPFKLW TEFNEDEEPT TTDAIILATG 

       130        140        150        160        170        180 
ASAKRLGLPG EETYWQRGIS ACAVCDGAVP IFRNKPLAVV GGGDSACEEA SFLTKYGSKV 

       190        200        210        220        230        240 
FMLVRKDHMR ASTIMQRRVE RNEKIEVLYN TAPVEAKGDG SLLDALRVRD TRTGEESDLP 

       250        260        270        280        290        300 
VNGLFYAIGH TPATQLVAGQ VDLDESGYVK TVPGSTLTNV PGLFAAGDVQ DSRYRQAVTS 

       310 
AGSGCMAALD AEKFLSELE 

« Hide

References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / NRRL Y-1056 / CBS 109.51.

Cross-references

Sequence databases

AE016816 Genomic DNA. Translation: AAS51119.1. Different initiation.
RefSeqNP_983295.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4619415.
KEGGago:AGOS_ACL109C.
NMPDRfig|33169.1.peg.940.

Organism-specific databases

AGDACL109C.

Phylogenomic databases

HOGENOMQ75CM8.

Enzyme and pathway databases

BRENDA1.8.1.9. 279361.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00469. PNDRDTASEII.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01292. TRX_reduct. 1 hit.
PROSITEPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRXB_ASHGO
AccessionPrimary (citable) accession number: Q75CM8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: November 9, 2004
Last modified: June 16, 2009
This is version 33 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents