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Reviewed, UniProtKB/Swiss-Prot O66790 (TRXB_AQUAE)

Last modified November 3, 2009. Version 70. 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
      Short name=TRXR
    EC=1.8.1.9
Gene names
Name: trxB
Ordered Locus Names: aq_500
OrganismAquifex aeolicus [Complete proteome] [HAMAP]
Taxonomic identifier63363 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length323 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 – 323323Thioredoxin reductase
PRO_0000166718

Regions

Nucleotide binding42 – 498FAD By similarity
Nucleotide binding286 – 29510FAD By similarity

Amino acid modifications

Disulfide bond143 ↔ 146Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O66790-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 363FC62EFDD03328

FASTA32335,101
        10         20         30         40         50         60 
MAVSLMQQPD KVYDVIIIGA GPAGTTAAIY TARAGWKTLV LYRAEADGAL GVTQKIENYP 

        70         80         90        100        110        120 
GVPGPLSGYE LLKIMREQAK SFGAEFVRGK VIATDLNSDP KKVYTIDGRE FRGKTIIVAS 

       130        140        150        160        170        180 
GAMERANKFK GEEEFLGRGV SYCGVCDAAF FKDQPVAVIG DDDYAIEEAE FIARFANKVF 

       190        200        210        220        230        240 
FVVPGSKIKA PPEVIEHFEK LPNVEILLRH RPIEIVGDQV VKGIKLKDLE KKEEKLLEVN 

       250        260        270        280        290        300 
GVFIFLGGTK PSVDFLMGQV EMTEGDCIVV NEEMMTSVPG VFAAGDVLCN EVKQAVVAAA 

       310        320 
MGCKAALAVD KFLSGKKKIV PQW 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

AE000657 Genomic DNA. Translation: AAC06756.1.
PIRB70345.
RefSeqNP_213350.1.

3D structure databases

HSSPHSSP built from PDB template 1TDE based on UniProtKB P09625.
ModBaseSearch...

Genome annotation databases

GeneID1193208.
GenomeReviewsGene locus aq_500 in contig AE000657_GR.
KEGGaae:aq_500.
NMPDRfig|224324.1.peg.365.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO66790.
OMAIGDIRNT.

Enzyme and pathway databases

BioCycAAEO224324:AQ_500-MON.
BRENDA1.8.1.9. 189781.

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_AQUAE
AccessionPrimary (citable) accession number: O66790
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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