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Reviewed, UniProtKB/Swiss-Prot Q2IEC3 (T23O_ANADE)

Last modified November 3, 2009. Version 22. 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
Gene names
Name: kynA
Ordered Locus Names: Adeh_3165
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring By similarity.

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 – 265265Tryptophan 2,3-dioxygenase
PRO_0000360080

Regions

Region13 – 175Substrate binding By similarity
Region38 – 425Substrate binding By similarity

Sites

Metal binding2231Iron (heme axial ligand) By similarity
Binding site1041Substrate By similarity
Binding site1111Heme By similarity
Binding site2371Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IEC3-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: FCE500FAEA6B7510

FASTA26529,720
        10         20         30         40         50         60 
MTDPSAHSAA LTYGSYLALD ELLAAQRPRS EEHDELLFIV VHQVYELWFK QVVHELTWLQ 

        70         80         90        100        110        120 
ERLHRGEGGH ALATLKRVLT ILKTVVAQVD VIETMTPRQF TAFRSRLEAA SGFQSAQFRV 

       130        140        150        160        170        180 
LEAMLGRRDD RMLAPYPPDG PGYARIAAAM AAPSLFDSLL RYLATQGFET PVVPEPRPAG 

       190        200        210        220        230        240 
WRQPSEAVQR VLLEVYRADG EAALVCERFV DLDEGVQEWR YRHVKMVERT IGDKPGTGGS 

       250        260 
AGARYLRSTL FTPAFPDLWA VRGAL 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000251 Genomic DNA. Translation: ABC82934.1.
RefSeqYP_466371.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2IEC3.

Genome annotation databases

GeneID3888971.
GenomeReviewsGene locus Adeh_3165 in contig CP000251_GR.
KEGGade:Adeh_3165.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2IEC3.
OMAQWSVLAT.

Enzyme and pathway databases

BioCycADEH290397:ADEH_3165-MON.

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_ANADE
AccessionPrimary (citable) accession number: Q2IEC3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: March 7, 2006
Last modified: November 3, 2009
This is version 22 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

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