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Q928B5 (TRXB_LISIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thioredoxin reductase

Short name=TRXR
EC=1.8.1.9
Gene names
Name:trxB
Ordered Locus Names:lin2621
OrganismListeria innocua [Complete proteome] [HAMAP]
Taxonomic identifier1642 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
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.

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

Chain1 – 319319Thioredoxin reductase
PRO_0000166735

Regions

Nucleotide binding37 – 448FAD By similarity
Nucleotide binding279 – 28810FAD By similarity

Amino acid modifications

Disulfide bond136 ↔ 139Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q928B5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: C77D54A952526CC1

FASTA31934,244
        10         20         30         40         50         60 
MASEEKIYDV IIIGAGPAGM TAALYTSRAD LDTLMIERGV PGGQMVNTAE VENYPGFDSI 

        70         80         90        100        110        120 
LGPDLSDKML SGAKQFGAEY AYGDIKEVID GKEFKTVTAG SKTYKARAII IATGAEHRKL 

       130        140        150        160        170        180 
GAAGEEELSG RGVSYCAVCD GAFFKNRELV VVGGGDSAVE EGTYLTRYAD KVTIVHRRDK 

       190        200        210        220        230        240 
LRAQQILQDR AFKDEKVDFI WNNTVEEIIG DGKKVTSVKL VSTVDGSESI MPVDGVFIYV 

       250        260        270        280        290        300 
GLVPLTKAFL SLGITDEEGY IVTDEEMRTN LPGIFAAGDV RAKSLRQIVT ATGDGGLAGQ 

       310 
NAQKYVEELK EALEAEAAK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL596173 Genomic DNA. Translation: CAC97848.1.
PIRAH1759.
RefSeqNP_471951.1. NC_003212.1.

3D structure databases

ProteinModelPortalQ928B5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1131452.
GenomeReviewsGene locus lin2621 in contig AL592022_GR.
KEGGlin:lin2621.
NMPDRfig|272626.1.peg.2604.
PATRIC20302159. VBILisInn102668_2692.

Organism-specific databases

GenoListLIN2621.
CMRSearch...

Phylogenomic databases

HOGENOMHBG669726.
OMAGEEREFP.
ProtClustDBCLSK2753262.

Enzyme and pathway databases

BioCycLINN272626:LIN2621-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_LISIN
AccessionPrimary (citable) accession number: Q928B5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 74 of the entry and version 1 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