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Reviewed, UniProtKB/Swiss-Prot P81433 (TRXB_BUCAP)

Last modified November 3, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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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: BUsg_304
OrganismBuchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]
Taxonomic identifier98794 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

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Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

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

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Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Thioredoxin reductase
PRO_0000166722

Regions

Nucleotide binding36 – 438FAD By similarity
Nucleotide binding288 – 29710FAD By similarity

Amino acid modifications

Disulfide bond136 ↔ 139Redox-active By similarity

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Sequences

Sequence LengthMass (Da)Tools
P81433-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: BB1A774645BCDBAD

FASTA31935,543
        10         20         30         40         50         60 
MELKNHKKII ILGSGPAGYT AAIYSSRANL NPLLITGINK GGQLMNTNEI ENWPGDFKKI 

        70         80         90        100        110        120 
TGPELMNRMH EHSLKFKTEI VYDNIISVEF KKKPFFLLGE YNKYTCDAVI IATGANPRYL 

       130        140        150        160        170        180 
GLSSENKFKG KGISTCAVCD GFFYKNKEIA VVGGGNTAIE ETLYLSNFVK KIYLIHRRNN 

       190        200        210        220        230        240 
FKAEKILIDR LLKIVKTKKV ILHLNSTIED ILGNNKGVTH LLIKNKNLKE KKKLKIAVSG 

       250        260        270        280        290        300 
LFVAIGYIPN TDIFTDQLKM KDGYIKIKKG THGNYTQTNI PGVFAAGDVI DHVYRQAITS 

       310 
SASGCMAALD SERYLNSLS

« Hide

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References

« Hide 'large scale' references
[1]"Nucleotide sequence of a DNA fragment from Buchnera aphidicola (Aphid endosymbiont) containing the genes aspS-trxB-serS-serC-aroA-rpsA-himD-tpiA."
Thao M.L., Baumann P.
Curr. Microbiol. 35:68-69(1997)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

L43549 Genomic DNA. Translation: AAC05433.1.
AE013218 Genomic DNA. Translation: AAM67858.1.
RefSeqNP_660647.1.

3D structure databases

HSSPHSSP built from PDB template 1F6M based on UniProtKB P09625.
ModBaseSearch...

Genome annotation databases

GeneID1005508.
GenomeReviewsGene locus BUsg_304 in contig AE013218_GR.
KEGGbas:BUsg304.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP81433.
OMAPSCGPCH.

Enzyme and pathway databases

BioCycBAPH198804:BUSG304-MON.

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...

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Entry information

Entry nameTRXB_BUCAP
AccessionPrimary (citable) accession number: P81433
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 69 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)

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Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

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