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Reviewed, UniProtKB/Swiss-Prot Q8CPY8 (TRXB_STAES)

Last modified June 16, 2009. Version 44. 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: SE_0547
OrganismStaphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]
Taxonomic identifier176280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length310 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 – 310310Thioredoxin reductase
PRO_0000166750

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
Q8CPY8-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D5D6853667137D8B

FASTA31033,544
        10         20         30         40         50         60 
MTEVDFDVAI IGAGPAGMTA AVYASRANLK TVMIERGMPG GQMANTEEVE NFPGFEMITG 

        70         80         90        100        110        120 
PDLSTKMFEH AKKFGAEYQY GDIKSVEDKG DYKVINLGNK EITAHAVIIS TGAEYKKIGV 

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

       190        200        210        220        230        240 
AQNILQERAF KNDKVDFIWS HTLKTINEKD GKVGSVTLES TKDGAEQTYD ADGVFIYIGM 

       250        260        270        280        290        300 
KPLTAPFKNL GITNDAGYIV TQDDMSTKVR GIFAAGDVRD KGLRQIVTAT GDGSIAAQSA 

       310 
ADYITELKDN 

« Hide

References

[1]"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)."
Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.
Mol. Microbiol. 49:1577-1593(2003) [PubMed: 12950922] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE015929 Genomic DNA. Translation: AAO04144.1.
RefSeqNP_764102.1.

3D structure databases

HSSPHSSP built from PDB template 1F6M based on UniProtKB P09625.
ModBaseSearch...

Genome annotation databases

GeneID1057773.
GenomeReviewsGene locus SE_0547 in contig AE015929_GR.
KEGGsep:SE0547.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8CPY8.
OMAQ8CPY8. FVGYDVN.

Enzyme and pathway databases

BioCycSEPI176280:SE_0547-MON.

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_STAES
AccessionPrimary (citable) accession number: Q8CPY8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: March 1, 2003
Last modified: June 16, 2009
This is version 44 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