Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thioredoxin reductase

Gene

trxB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 438FAD1 Publication
Nucleotide bindingi287 – 29610FAD1 Publication

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: EcoCyc
  • thioredoxin-disulfide reductase activity Source: CACAO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciEcoCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER.
ECOL316407:JW0871-MONOMER.
MetaCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER.
BRENDAi1.8.1.9. 2026.
SABIO-RKP0A9P4.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase (EC:1.8.1.9)
Short name:
TRXR
Gene namesi
Name:trxB
Ordered Locus Names:b0888, JW0871
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11032. trxB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 321320Thioredoxin reductasePRO_0000166729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi136 ↔ 139Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0A9P4.
PaxDbiP0A9P4.
PRIDEiP0A9P4.

2D gel databases

SWISS-2DPAGEP0A9P4.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
trxAP0AA252EBI-1029826,EBI-368542

Protein-protein interaction databases

BioGridi4261715. 36 interactions.
DIPiDIP-6168N.
IntActiP0A9P4. 15 interactions.
STRINGi511145.b0888.

Chemistry

BindingDBiP0A9P4.

Structurei

Secondary structure

1
321
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Helixi16 – 2611Combined sources
Turni27 – 293Combined sources
Beta strandi33 – 353Combined sources
Helixi42 – 465Combined sources
Helixi62 – 7514Combined sources
Beta strandi79 – 813Combined sources
Beta strandi85 – 895Combined sources
Beta strandi91 – 10111Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi115 – 1173Combined sources
Helixi123 – 1275Combined sources
Turni130 – 1323Combined sources
Beta strandi133 – 1353Combined sources
Helixi137 – 1404Combined sources
Helixi141 – 1444Combined sources
Beta strandi147 – 1526Combined sources
Helixi156 – 16510Combined sources
Turni166 – 1683Combined sources
Beta strandi169 – 1757Combined sources
Beta strandi177 – 1804Combined sources
Helixi185 – 19612Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi207 – 2137Combined sources
Beta strandi215 – 22410Combined sources
Beta strandi227 – 2293Combined sources
Beta strandi233 – 2364Combined sources
Beta strandi238 – 2425Combined sources
Beta strandi246 – 2494Combined sources
Helixi251 – 2533Combined sources
Turni254 – 2563Combined sources
Beta strandi269 – 2724Combined sources
Beta strandi282 – 2843Combined sources
Helixi286 – 2894Combined sources
Beta strandi291 – 2933Combined sources
Helixi296 – 31419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A9P4.
SMRiP0A9P4. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9P4.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105C3M. Bacteria.
COG0492. LUCA.
HOGENOMiHOG000072912.
InParanoidiP0A9P4.
KOiK00384.
OMAiGQLEMNN.
OrthoDBiEOG65XN2W.
PhylomeDBiP0A9P4.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9P4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV
60 70 80 90 100
ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD
110 120 130 140 150
NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA
160 170 180 190 200
VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI
210 220 230 240 250
ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT
260 270 280 290 300
AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA
310 320
GTGCMAALDA ERYLDGLADA K
Length:321
Mass (Da):34,623
Last modified:January 23, 2007 - v2
Checksum:i8E5AF86FB195CC82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA28074. RDECT.
RefSeqiNP_415408.1. NC_000913.3.
WP_000537418.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73974; AAC73974; b0888.
BAA35613; BAA35613; BAA35613.
GeneIDi949054.
KEGGiecj:JW0871.
eco:b0888.
PATRICi32116985. VBIEscCol129921_0917.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA28074. RDECT.
RefSeqiNP_415408.1. NC_000913.3.
WP_000537418.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A9P4.
SMRiP0A9P4. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261715. 36 interactions.
DIPiDIP-6168N.
IntActiP0A9P4. 15 interactions.
STRINGi511145.b0888.

Chemistry

BindingDBiP0A9P4.
DrugBankiDB03147. Flavin adenine dinucleotide.

2D gel databases

SWISS-2DPAGEP0A9P4.

Proteomic databases

EPDiP0A9P4.
PaxDbiP0A9P4.
PRIDEiP0A9P4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73974; AAC73974; b0888.
BAA35613; BAA35613; BAA35613.
GeneIDi949054.
KEGGiecj:JW0871.
eco:b0888.
PATRICi32116985. VBIEscCol129921_0917.

Organism-specific databases

EchoBASEiEB1025.
EcoGeneiEG11032. trxB.

Phylogenomic databases

eggNOGiENOG4105C3M. Bacteria.
COG0492. LUCA.
HOGENOMiHOG000072912.
InParanoidiP0A9P4.
KOiK00384.
OMAiGQLEMNN.
OrthoDBiEOG65XN2W.
PhylomeDBiP0A9P4.

Enzyme and pathway databases

BioCyciEcoCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER.
ECOL316407:JW0871-MONOMER.
MetaCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER.
BRENDAi1.8.1.9. 2026.
SABIO-RKP0A9P4.

Miscellaneous databases

EvolutionaryTraceiP0A9P4.
PROiP0A9P4.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-26.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  10. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BOND, FAD BINDING SITES, COFACTOR.
  11. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  12. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXA, SUBUNIT.

Entry informationi

Entry nameiTRXB_ECOLI
AccessioniPrimary (citable) accession number: P0A9P4
Secondary accession number(s): P09625
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.