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UniProtKB/Swiss-Prot entry P0A9P5

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

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Entry information
Entry name TRXB_ECO57
Primary accession number P0A9P5
Secondary accession number P09625
Integrated into Swiss-Prot on July 19, 2005
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 28)
Name and origin of the protein
Protein name Thioredoxin reductase
Synonyms TRXR
EC 1.8.1.9
Gene name
Name: trxB
OrderedLocusNames: Z1232, ECs0973
From
Escherichia coli O157:H7 [TaxID: 83334] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
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
AE005174; AAG55375.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB34396.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C85614; C85614.
E90750; E90750.
RefSeq NP_286765.1; -.
NP_309000.1; -.
3D structure databases
SMR P0A9P5; 2-317.
ModBase P0A9P5.
Enzyme and pathway databases
BioCyc ECOL83334:ECS0973-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 917715; -.
958846; -.
GenomeReviews AE005174_GR; Z1232.
BA000007_GR; ECs0973.
KEGG ece:Z1232; -.
ecs:ECs0973; -.
Phylogenomic databases
HOGENOM P0A9P5; -.
Genome annotation databases
CMR P0A9P5; Z1232.
Other
ProtoNet P0A9P5.
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
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   321  320     Thioredoxin reductase. PRO_0000166730
NP_BIND   36    43  8     FAD (By similarity). 
NP_BIND   287   296  10     FAD (By similarity). 
DISULFID   136   139        Redox-active (By similarity). 
Sequence information
Length: 321 AA [This is the length of the unprocessed precursor] Molecular weight: 34623 Da [This is the MW of the unprocessed precursor] CRC64: 8E5AF86FB195CC82 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL 

        70         80         90        100        110        120 
TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL 

       130        140        150        160        170        180 
GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG 

       190        200        210        220        230        240 
FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL 

       250        260        270        280        290        300 
FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA 

       310        320 
GTGCMAALDA ERYLDGLADA K
P0A9P5 in FASTA format

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