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Reviewed, UniProtKB/Swiss-Prot Q5HHQ4 (TRXB_STAAC)

Last modified February 9, 2010. Version 38. 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: SACOL0829
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
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

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 – 311311Thioredoxin reductase
PRO_0000166744

Regions

Nucleotide binding35 – 428FAD By similarity
Nucleotide binding277 – 28610FAD By similarity

Amino acid modifications

Disulfide bond134 ↔ 137Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HHQ4-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 1A337DE3736C9265

FASTA31133,616
        10         20         30         40         50         60 
MTEIDFDIAI IGAGPAGMTA AVYASRANLK TVMIERGIPG GQMANTEEVE NFPGFEMITG 

        70         80         90        100        110        120 
PDLSTKMFEH AKKFGAVYQY GDIKSVEDKG EYKVINFGNK ELTAKAVIIA TGAEYKKIGV 

       130        140        150        160        170        180 
PGEQELGGRG VSYCAVCDGA FFKNKRLFVI GGGDSAVEEG TFLTKFADKV TIVHRRDELR 

       190        200        210        220        230        240 
AQRILQDRAF KNDKIDFIWS HTLKSINEKD GKVGSVTLTS TKDGSEETHE ADGVFIYIGM 

       250        260        270        280        290        300 
KPLTAPFKDL GITNDVGYIV TKDDMTTSVP GIFAAGDVRD KGLRQIVTAT GDGSIAAQSA 

       310 
AEYIEHLNDQ A 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000046 Genomic DNA. Translation: AAW36385.1.
RefSeqYP_185703.1.

3D structure databases

SMRQ5HHQ4. Positions 2-307.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HHQ4.

Genome annotation databases

GeneID3238649.
GenomeReviewsGene locus SACOL0829 in contig CP000046_GR.
KEGGsac:SACOL0829.
TIGRSACOL0829.

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHBG669726.
OMATRFANKV.

Enzyme and pathway databases

BioCycSAUR93062:SACOL0829-MONOMER.

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.
TIGRFAMsTIGR01292. TRX_reduct. 1 hit.
PROSITEPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRXB_STAAC
AccessionPrimary (citable) accession number: Q5HHQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: February 9, 2010
This is version 38 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