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Reviewed, UniProtKB/Swiss-Prot P0A9P4 (TRXB_ECOLI)

Last modified June 16, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · 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: b0888, JW0871
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

nadEP188431EBI-1029826,EBI-548960

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 321320Thioredoxin reductase
PRO_0000166729

Regions

Nucleotide binding36 – 438FAD
Nucleotide binding287 – 29610FAD

Amino acid modifications

Disulfide bond136 ↔ 139Redox-active Ref.9

Secondary structure

............................................................ 321
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9P4-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8E5AF86FB195CC82

FASTA32134,623
        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 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases."
Russel M., Model P.
J. Biol. Chem. 263:9015-9019(1988) [PubMed: 3288628] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"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."
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. expand/collapse author list , 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.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Molecular characterization of the Escherichia coli htrD gene: cloning, sequence, regulation, and involvement with cytochrome d oxidase."
Delaney J.M., Wall D., Georgopoulos C.
J. Bacteriol. 175:166-175(1993) [PubMed: 8380150] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-321.
Strain: K12.
[6]"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."
Poole R.K., Hatch L., Cleeter M.W.J., Gibson F., Cox G.B., Wu G.
Mol. Microbiol. 10:421-430(1993) [PubMed: 7934832] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-321.
[7]"Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit."
Ueshima R., Fujita N., Ishihama A.
Biochem. Biophys. Res. Commun. 184:634-639(1992) [PubMed: 1575737] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26.
[8]"Convergent evolution of similar function in two structurally divergent enzymes."
Kuriyan J., Krishna T.S.R., Wong L., Guenther B., Pahler A., Williams C.H. Jr., Model P.
Nature 352:172-174(1991) [PubMed: 2067578] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[9]"Crystal structure of Escherichia coli thioredoxin reductase refined at 2-A resolution. Implications for a large conformational change during catalysis."
Waksman G., Krishna T.S.R., Williams C.H. Jr., Kuriyan J.
J. Mol. Biol. 236:800-816(1994) [PubMed: 8114095] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BOND.
[10]"Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor."
Lennon B.W., Williams C.H. Jr., Ludwig M.L.
Protein Sci. 8:2366-2379(1999) [PubMed: 10595539] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[11]"Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase."
Lennon B.W., Williams C.H. Jr., Ludwig M.L.
Science 289:1190-1194(2000) [PubMed: 10947986] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXA.

Cross-references

Sequence databases

J03762 Genomic DNA. Translation: AAA24697.1.
U00096 Genomic DNA. Translation: AAC73974.1.
AP009048 Genomic DNA. Translation: BAA35613.1.
L21749 Genomic DNA. Translation: AAA66170.1.
M95935 Genomic DNA. No translation available.
PIRRDECT. A28074.
RefSeqAP_001518.1.
NP_415408.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CL0X-ray2.50A2-321[»]
1F6MX-ray2.95A/B/E/F2-321[»]
1TDEX-ray2.10A2-317[»]
1TDFX-ray2.30A2-317[»]
1TRBX-ray2.00A2-321[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP0A9P4. 5 interactions.

2-D gel databases

SWISS-2DPAGEP0A9P4.
ECO2DBASED031.5. 6TH EDITION.

Genome annotation databases

GeneID949054.
GenomeReviewsGene locus JW0871 in contig AP009048_GR.
Gene locus b0888 in contig U00096_GR.
KEGGecj:JW0871.
eco:b0888.

Organism-specific databases

EchoBASEEB1025.
EcoGeneEG11032. trxB.
CMRSearch...

Phylogenomic databases

HOGENOMP0A9P4.
OMAP0A9P4. PSCGPCH.

Enzyme and pathway databases

BioCycEcoCyc:THIOREDOXIN-REDUCT-NADPH-MON.
MetaCyc:THIOREDOXIN-REDUCT-NADPH-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_ECOLI
AccessionPrimary (citable) accession number: P0A9P4
Secondary accession number(s): P09625
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents