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Reviewed, UniProtKB/Swiss-Prot Q95NN1 (T23O_TRICA)

Last modified September 1, 2009. Version 25. 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

Names and origin

Protein namesRecommended name:
    Tryptophan 2,3-dioxygenase
      Short name=TDO
    EC=1.13.11.11
Alternative name(s):
    Tryptophan pyrrolase
      Short name=Tryptophanase
    Tryptophan oxygenase
      Short name=TRPO
      Short name=TO
    Tryptamin 2,3-dioxygenase
OrganismTribolium castaneum (Red flour beetle)
Taxonomic identifier7070 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaCucujiformiaTenebrionidaeTribolium

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring By similarity. Required for normal eye pigmentation.

Catalytic activity

L-tryptophan + O2 = N-formyl-L-kynurenine.

Cofactor

Binds 2 heme groups per tetramer By similarity.

Pathway

Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the tryptophan 2,3-dioxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Tryptophan 2,3-dioxygenase
PRO_0000360886

Regions

Region24 – 285Substrate binding By similarity
Region54 – 585Substrate binding By similarity
Coiled coil205 – 23531 Potential

Sites

Metal binding3091Iron (heme axial ligand) By similarity
Binding site1241Substrate By similarity
Binding site1311Heme By similarity
Binding site3241Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q95NN1-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 96A34C73ED0F1F03

FASTA38845,423
        10         20         30         40         50         60 
MSCPLRPSEA QEGDQLSEEC GMLYGEYLML DKILEAQRLL SEQNNQPVHD EHLFIVTHQA 

        70         80         90        100        110        120 
YELWFKQIIY ELDSIRNIFS DVLEESQTLE ILKRLNRVVL ILKVLVDQVM ILETMTPLDF 

       130        140        150        160        170        180 
MDFRCYLRPA SGFQSLQFRL LENKLGVRQE NRVKYNQNYS KVFGNDEKAL EQIAKSEKEP 

       190        200        210        220        230        240 
SLTDLVQRWL ERTPGLELEG FNFWGKYQKA VEKLLTEQKE LAEKEEAETL KRYKLNDLEK 

       250        260        270        280        290        300 
RREVYESIFK VEVHEALMSR GERRFSHKAL QGAIMITFYR DEPRFSQPHQ ILTLLMDIDS 

       310        320        330        340        350        360 
LITKWRYNHV LMVQRMIGSS QLGTGGSSGY QYLRSTLSDR YKVFVDLFNL STFLIPRSYI 

       370        380 
PPLSTSMRSH LCNWGSANST NIVSNGNN 

« Hide

References

[1]"Cloning and characterization of the Tribolium castaneum eye-color genes encoding tryptophan oxygenase and kynurenine 3-monooxygenase."
Lorenzen M.D., Brown S.J., Denell R.E., Beeman R.W.
Genetics 160:225-234(2002) [PubMed: 11805058] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: GA-1 and GA-2.

Cross-references

Sequence databases

AY052390 mRNA. Translation: AAL15464.1.
AY052392 Genomic DNA. Translation: AAL15466.1.
RefSeqNP_001034499.1.
UniGeneTca.5753

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID654844.
KEGGtca:654844.

Organism-specific databases

CTD654844.

Family and domain databases

InterProIPR004981. Trp_2_3_dOase.
[Graphical view]
PANTHERPTHR10138. Trp_2_3_dOase. 1 hit.
PfamPF03301. Trp_dioxygenase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameT23O_TRICA
AccessionPrimary (citable) accession number: Q95NN1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: December 1, 2001
Last modified: September 1, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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