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P52213 (TRXB_CLOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 69. 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
OrganismClostridium litorale (Bacterium W6)
Taxonomic identifier1557 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length315 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
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 – 315315Thioredoxin reductase
PRO_0000166727

Regions

Nucleotide binding34 – 418FAD By similarity
Nucleotide binding282 – 29110FAD By similarity

Amino acid modifications

Disulfide bond134 ↔ 137Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P52213 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 2CA55D36E579E2EF

FASTA31533,946
        10         20         30         40         50         60 
MENVYDIAII GSGPAGLAAA LYGARAKMKT LLLEGMKVGG QIVITHEVAN YPGSVPEATG 

        70         80         90        100        110        120 
PSLIGRMEEQ VEEFGAERVM DNIVDVDFTD KIKVLKGAKG EYKAKAVIVA TGASPKLAGC 

       130        140        150        160        170        180 
PGEKELTGKG VSYCATCDAD FFEDMEVFVI GGGDTAVEEA MFLTKFARKV TIVHRRAELR 

       190        200        210        220        230        240 
AAKSIQEKAF KNEKLNFMWN TVIEEIKGDG IVESAVFKNR ETGEVTEFVA PEEDGTFGIF 

       250        260        270        280        290        300 
VFIGYDPKSA LVEGKLELDE TGYIPTDDNM KTNVEGVFAA GDIRVKSLRQ VVTATADGAI 

       310 
AAVQAEKYIE ELFAE 

« Hide

References

[1]"Glycine reductase of Clostridium litorale. Cloning, sequencing, and molecular analysis of the grdAB operon that contains two in-frame TGA codons for selenium incorporation."
Kreimer S., Andreesen J.R.
Eur. J. Biochem. 234:192-199(1995) [PubMed: 8529640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24268 Genomic DNA. Translation: AAC43575.1.
PIRS63990.

3D structure databases

ProteinModelPortalP52213.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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]
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_CLOLI
AccessionPrimary (citable) accession number: P52213
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 21, 2011
This is version 69 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