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P0A9P5 (TRXB_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thioredoxin reductase
Short name=TRXR
EC=1.8.1.9
Gene names
Name:trxB
Ordered Locus Names:Z1232, ECs0973
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond By similarity.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processremoval of superoxide radicals

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

thioredoxin-disulfide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 321320Thioredoxin reductase
PRO_0000166730

Regions

Nucleotide binding36 – 438FAD By similarity
Nucleotide binding287 – 29610FAD By similarity

Amino acid modifications

Disulfide bond136 ↔ 139Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A9P5 [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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG55375.1.
BA000007 Genomic DNA. Translation: BAB34396.1.
PIRC85614.
E90750.
RefSeqNP_286765.1. NC_002655.2.
NP_309000.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A9P5.
SMRP0A9P5. Positions 2-316.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000028261; EBESCP00000027154; EBESCG00000027312.
EBESCT00000059704; EBESCP00000057532; EBESCG00000058751.
GeneID917715.
958846.
GenomeReviewsGene locus Z1232 in contig AE005174_GR.
Gene locus ECs0973 in contig BA000007_GR.
KEGGece:Z1232.
ecs:ECs0973.
PATRIC18351197. VBIEscCol44059_1102.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009144.
HOGENOMHBG669726.
OMAVMGAFIA.
ProtClustDBPRK10262.

Enzyme and pathway databases

BioCycECOL83334:ECS0973-MONOMER.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
KOK00384.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00469. PNDRDTASEII.
TIGRFAMsTIGR01292. TRX_reduct. 1 hit.
PROSITEPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRXB_ECO57
AccessionPrimary (citable) accession number: P0A9P5
Secondary accession number(s): P09625
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 50 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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