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UniProtKB/Swiss-Prot entry P0A9P4


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

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Entry information
Entry name TRXB_ECOLI
Primary accession number P0A9P4
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    September 2, 2008 (Entry version 38)
Name and origin of the protein
Protein name Thioredoxin reductase
Synonyms TRXR
EC 1.8.1.9
Gene name
Name: trxB
OrderedLocusNames: b0888, JW0871
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3288628 [NCBI, ExPASy, EBI, Israel, Japan]
Russel M., Model P.;
"Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases.";
J. Biol. Chem. 263:9015-9019(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-321.
STRAIN=K12;
PubMed=8380150 [NCBI, ExPASy, EBI, Israel, Japan]
Delaney J.M., Wall D., Georgopoulos C.;
"Molecular characterization of the Escherichia coli htrD gene: cloning, sequence, regulation, and involvement with cytochrome d oxidase.";
J. Bacteriol. 175:166-175(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-321.
PubMed=7934832 [NCBI, ExPASy, EBI, Israel, Japan]
Poole R.K., Hatch L., Cleeter M.W.J., Gibson F., Cox G.B., Wu G.;
"Cytochrome bd biosynthesis in Escherichia coli: the sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter.";
Mol. Microbiol. 10:421-430(1993).
[7]
PROTEIN SEQUENCE OF 2-26.
DOI=10.1016/0006-291X(92)90636-Y; PubMed=1575737 [NCBI, ExPASy, EBI, Israel, Japan]
Ueshima R., Fujita N., Ishihama A.;
"Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit.";
Biochem. Biophys. Res. Commun. 184:634-639(1992).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1038/352172a0; PubMed=2067578 [NCBI, ExPASy, EBI, Israel, Japan]
Kuriyan J., Krishna T.S.R., Wong L., Guenther B., Pahler A., Williams C.H. Jr., Model P.;
"Convergent evolution of similar function in two structurally divergent enzymes.";
Nature 352:172-174(1991).
[9]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DISULFIDE BOND.
DOI=10.1006/jmbi.1994.1190; PubMed=8114095 [NCBI, ExPASy, EBI, Israel, Japan]
Waksman G., Krishna T.S.R., Williams C.H. Jr., Kuriyan J.;
"Crystal structure of Escherichia coli thioredoxin reductase refined at 2-A resolution. Implications for a large conformational change during catalysis.";
J. Mol. Biol. 236:800-816(1994).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=10595539 [NCBI, ExPASy, EBI, Israel, Japan]
Lennon B.W., Williams C.H. Jr., Ludwig M.L.;
"Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor.";
Protein Sci. 8:2366-2379(1999).
[11]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXA.
DOI=10.1126/science.289.5482.1190; PubMed=10947986 [NCBI, ExPASy, EBI, Israel, Japan]
Lennon B.W., Williams C.H. Jr., Ludwig M.L.;
"Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase.";
Science 289:1190-1194(2000).
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
J03762; AAA24697.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73974.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35613.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L21749; AAA66170.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M95935; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR A28074; RDECT.
RefSeq AP_001518.1; -.
NP_415408.1; -.
3D structure databases
PDB
1CL0; X-ray; 2.50 A; A=1-321.[ExPASy / RCSB / EBI]
1F6M; X-ray; 2.95 A; A/B/E/F=1-321.[ExPASy / RCSB / EBI]
1TDE; X-ray; 2.10 A; A=1-317.[ExPASy / RCSB / EBI]
1TDF; X-ray; 2.30 A; A=1-317.[ExPASy / RCSB / EBI]
1TRB; X-ray; 2.00 A; A=1-321.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CL0; -.
1F6M; -.
1TDE; -.
1TDF; -.
1TRB; -.
ModBase P0A9P4.
Protein-protein interaction databases
IntAct P0A9P4; -.
Enzyme and pathway databases
BioCyc EcoCyc:THIOREDOXIN-REDUCT-NADPH-MON; -.
MetaCyc:THIOREDOXIN-REDUCT-NADPH-MON; -.
2D gel databases
SWISS-2DPAGE P0A9P4; -.
ECO2DBASE D031.5; 6TH EDITION.
Organism-specific databases
EchoBASE EB1025; -.
EcoGene EG11032; trxB.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
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.
BLOCKS P0A9P4.
Genome annotation databases
GeneID 949054; -.
GenomeReviews U00096_GR; b0888.
AP009048_GR; JW0871.
KEGG ecj:JW0871; -.
eco:b0888; -.
Phylogenomic databases
HOGENOM P0A9P4; -.
Other
LinkHub P0A9P4; -.
Genome annotation databases
CMR P0A9P4; b0888.
Other
ProtoNet P0A9P4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   321  320     Thioredoxin reductase. PRO_0000166729
NP_BIND   36    43  8     FAD. 
NP_BIND   287   296  10     FAD. 
DISULFID   136   139        Redox-active. 
STRAND   4    12  9      
HELIX   16    26  11      
TURN   27    29  3      
STRAND   33    35  3      
HELIX   43    46  4      
HELIX   62    75  14      
STRAND   79    81  3      
STRAND   85    89  5      
STRAND   91   101  11      
STRAND   103   111  9      
STRAND   115   117  3      
HELIX   123   127  5      
TURN   130   132  3      
STRAND   133   135  3      
HELIX   137   140  4      
HELIX   141   144  4      
STRAND   147   152  6      
HELIX   156   165  10      
TURN   166   168  3      
STRAND   169   180  12      
HELIX   185   196  12      
STRAND   197   204  8      
STRAND   207   213  7      
STRAND   215   224  10      
STRAND   234   236  3      
STRAND   238   242  5      
STRAND   246   249  4      
HELIX   251   253  3      
TURN   254   256  3      
STRAND   269   272  4      
STRAND   282   284  3      
HELIX   286   288  3      
HELIX   296   314  19      
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 

P0A9P4 in FASTA format

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