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UniProtKB/Swiss-Prot entry Q8CPY8

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TRXB_STAES
Primary accession number Q8CPY8
Secondary accession numbers None
Integrated into Swiss-Prot on November 28, 2003
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 40)
Name and origin of the protein
Protein name Thioredoxin reductase
Synonyms TRXR
EC 1.8.1.9
Gene name
Name: trxB
OrderedLocusNames: SE_0547
From
Staphylococcus epidermidis (strain ATCC 12228) [TaxID: 176280] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1046/j.1365-2958.2003.03671.x; PubMed=12950922 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228).";
Mol. Microbiol. 49:1577-1593(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE015929; AAO04144.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_764102.1; -.
3D structure databases
HSSP P09625; 1F6M. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q8CPY8.
Enzyme and pathway databases
BioCyc SEPI176280:SE_0547-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004791; Molecular function: thioredoxin-disulfide reductase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019430; Biological process: removal of superoxide radicals (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000759; Adrndx_reductase.
IPR013027; 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_reduct.
Graphical view of domain structure.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01292; TRX_reduct; 1.
PROSITE PS00573; PYRIDINE_REDOX_2; 1.
Genome annotation databases
GeneID 1057773; -.
GenomeReviews AE015929_GR; SE_0547.
KEGG sep:SE0547; -.
Phylogenomic databases
HOGENOM Q8CPY8; -.
Genome annotation databases
CMR Q8CPY8; SE_0547.
Other
ProtoNet Q8CPY8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   310  310     Thioredoxin reductase. PRO_0000166750
NP_BIND   35    42  8     FAD (By similarity). 
NP_BIND   277   286  10     FAD (By similarity). 
DISULFID   134   137        Redox-active (By similarity). 
Sequence information
Length: 310 AA [This is the length of the unprocessed precursor] Molecular weight: 33544 Da [This is the MW of the unprocessed precursor] CRC64: D5D6853667137D8B [This is a checksum on the sequence] 
        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
Q8CPY8 in FASTA format

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