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Reviewed, UniProtKB/Swiss-Prot P50971 (TRXB_EUBAC)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · 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
OrganismEubacterium acidaminophilum
Taxonomic identifier1731 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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 termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

removal of superoxide radicals

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

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_0000166731

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
P50971-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 145B0EABB2B8A7FA

FASTA31534,034
        10         20         30         40         50         60 
MENVYDLAII GSGPAGLAAA LYGARAKMKT IMIEGQKVGG QIVITHEVAN YPGSVREATG 

        70         80         90        100        110        120 
PSLIERMEEQ ANEFGAEKVM DKIVDVDLDG KIKVIKGEKA EYKAKSVILA TGAAPRLAGC 

       130        140        150        160        170        180 
PGEQELTGKG VSYCATCDAD FFEDMEVFVV GGGDTAVEEA MYLAKFARKV TIVHRRDELR 

       190        200        210        220        230        240 
AAKSIQEKAF KNPKLDFMWN SAIEEIKGDG IVESAVFKNL VTGETTEYFA NEEDGTFGIF 

       250        260        270        280        290        300 
VFIGYIPKSD VFKGKITLDD AGYIITDDNM KTNVEGVFAA GDIRVKSLRQ VVTACADGAI 

       310 
AATQAEKYVE ANFEE 

« Hide

References

[1]"Components of glycine reductase from Eubacterium acidaminophilum. Cloning, sequencing and identification of the genes for thioredoxin reductase, thioredoxin and selenoprotein PA."
Luebbers M., Andreesen J.R.
Eur. J. Biochem. 217:791-798(1993) [PubMed: 8223622] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 49065 / DSM 3953 / al-2.
[2]Andreesen J.R.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 275.
[3]"Isolation of an atypically small lipoamide dehydrogenase involved in the glycine decarboxylase complex from Eubacterium acidaminophilum."
Freundenberg W., Dietrichs D., Lebertz H., Andreesen J.R.
J. Bacteriol. 171:1346-1354(1989) [PubMed: 2537814] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-54.

Cross-references

Sequence databases

L04500 Genomic DNA. Translation: AAB93303.1.
PIRD35156. S38988.

3D structure databases

HSSPHSSP built from PDB template 1TDE based on UniProtKB P09625.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.8.1.9. 256975.

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_EUBAC
AccessionPrimary (citable) accession number: P50971
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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