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Reviewed, UniProtKB/Swiss-Prot O83790 (TRXB_TREPA)

Last modified June 16, 2009. Version 67. 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
Ordered Locus Names: TP_0814
OrganismTreponema pallidum [Complete proteome] [HAMAP]
Taxonomic identifier160 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 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 – 307307Thioredoxin reductase
PRO_0000166754

Regions

Nucleotide binding34 – 418FAD By similarity
Nucleotide binding275 – 28410FAD By similarity

Amino acid modifications

Disulfide bond134 ↔ 137Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O83790-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 2519A5BA3BB4E012

FASTA30732,868
        10         20         30         40         50         60 
METDYDVIIV GAGAAGLSAA QYACRANLRT LVIESKAHGG QALLIDSLEN YPGYATPISG 

        70         80         90        100        110        120 
FEYAENMKKQ AVAFGAQIAY EEVTTIGKRD SVFHITTGTG AYTAMSVILA TGAEHRKMGI 

       130        140        150        160        170        180 
PGESEFLGRG VSYCATCDGP FFRNKHVVVI GGGDAACDES LVLSRLTDRV TMIHRRDTLR 

       190        200        210        220        230        240 
AQKAIAERTL KNPHIAVQWN TTLEAVRGET KVSSVLLKDV KTGETRELAC DAVFFFIGMV 

       250        260        270        280        290        300 
PITGLLPDAE KDSTGYIVTD DEMRTSVEGI FAAGDVRAKS FRQVITATSD GALAAHAAAS 


YIDTLQN 

« Hide

Cross-references

Sequence databases

AE000520 Genomic DNA. Translation: AAC65780.1.
PIRC71278.
RefSeqNP_219250.1.

3D structure databases

HSSPHSSP built from PDB template 1VDC based on UniProtKB Q39243.
ModBaseSearch...

Protein-protein interaction databases

IntActO83790. 9 interactions.

Genome annotation databases

GeneID2610892.
GenomeReviewsGene locus TP_0814 in contig AE000520_GR.
KEGGtpa:TP0814.
NMPDRfig|243276.1.peg.809.
TIGRTP_0814.

Phylogenomic databases

HOGENOMO83790.
OMAO83790. SYTIENY.

Enzyme and pathway databases

BioCycTPAL243276:TP_0814-MON.
BRENDA1.8.1.9. 142600.

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_TREPA
AccessionPrimary (citable) accession number: O83790
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: June 16, 2009
This is version 67 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