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UniProtKB/Swiss-Prot entry Q68WT3

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

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Entry information
Entry name TRXB_RICTY
Primary accession number Q68WT3
Secondary accession numbers None
Integrated into Swiss-Prot on February 6, 2007
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 32)
Name and origin of the protein
Protein name Thioredoxin reductase
Synonyms TRXR
EC 1.8.1.9
Gene name
Name: trxB
OrderedLocusNames: RT0432
From
Rickettsia typhi [TaxID: 785] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC VR-144 / Wilmington;
DOI=10.1128/JB.186.17.5842-5855.2004; PubMed=15317790 [NCBI, ExPASy, EBI, Israel, Japan]
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C., Yu X.-J., Walker D.H., Weinstock G.M.;
"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae.";
J. Bacteriol. 186:5842-5855(2004).
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
AE017197; AAU03909.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_067391.1; -.
3D structure databases
ModBase Q68WT3.
Enzyme and pathway databases
BioCyc RTYP257363:RT0432-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 2958952; -.
GenomeReviews AE017197_GR; RT0432.
KEGG rty:RT0432; -.
Phylogenomic databases
HOGENOM Q68WT3; -.
Genome annotation databases
CMR Q68WT3; RT0432.
Other
ProtoNet Q68WT3.
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_0000274792
NP_BIND   34    41  8     FAD (By similarity). 
NP_BIND   281   290  10     FAD (By similarity). 
DISULFID   135   138        Redox-active (By similarity). 
Sequence information
Length: 310 AA [This is the length of the unprocessed precursor] Molecular weight: 33699 Da [This is the MW of the unprocessed precursor] CRC64: C1D1EB4A96A5DE49 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKITTKVLII GSGPAGLSAA IYTARSSLKP ILINGMQPGG QLTMTTDVEN YPGFAKTIQG 

        70         80         90        100        110        120 
PWLMEQMSIQ AKNVGTEIIN DYVERVDLSK RPFKIFTGTG NKYEADSIII CTGAESKWLG 

       130        140        150        160        170        180 
ITSEQEFRGF GVSSCAICDG FFFKNQDIVV VGGGNSALEE ALYLTNHANK VTVVHRRNSF 

       190        200        210        220        230        240 
RAEKILQDRL FKNPKISVIW DHVIDEIVGS NQPKTVTGVK IKNVYTNEIN LVNCSGVFIA 

       250        260        270        280        290        300 
IGHTPNTTLF NGQIAIDDDN YIITQTGSTR TSVEGVFAAG DVQDKIYRQA ITAAASGCMA 

       310 
ALEVAKFLNK
Q68WT3 in FASTA format

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