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Q62M99 (T23O_BURMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tryptophan 2,3-dioxygenase

Short name=TDO
EC=1.13.11.11
Alternative name(s):
Tryptamin 2,3-dioxygenase
Tryptophan oxygenase
Short name=TO
Short name=TRPO
Tryptophan pyrrolase
Tryptophanase
Gene names
Name:kynA
Ordered Locus Names:BMA0351
OrganismBurkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]
Taxonomic identifier13373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
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 caution

The sequence AAU49146.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 306306Tryptophan 2,3-dioxygenase
PRO_0000360105

Regions

Region50 – 545Substrate binding By similarity
Region75 – 795Substrate binding By similarity

Sites

Metal binding2641Iron (heme axial ligand) By similarity
Binding site1371Substrate By similarity
Binding site1411Substrate By similarity
Binding site1481Heme By similarity
Binding site2781Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q62M99 [UniParc].

Last modified January 20, 2009. Version 2.
Checksum: 2D8AB0B21020B95A

FASTA30634,902
        10         20         30         40         50         60 
MQPPGDDAAP RCPFAGAHAP DAPHVPEAAG DDVQAGWHRA QLDFSQSMSY GDYLSLDPIL 

        70         80         90        100        110        120 
DAQHPRSPDH NEMLFIIQHQ TSELWMKLAL YELRAALASI RDDALPPAFK MLARVSRVLE 

       130        140        150        160        170        180 
QLVQAWNVLA TMTPSEYSAM RPYLGASSGF QSYQYRELEF ILGNKNAQML RPHAHRPAIH 

       190        200        210        220        230        240 
AHLEASLQAP SLYDEVIRLL ARRGFPIAPE RLDADWTQPT RHDRTVETAW LAVYREPNAH 

       250        260        270        280        290        300 
WELYEMAEEL VDLEDAFRQW RFRHVTTVER IIGFKQGTGS TSGAPYLRKM LDVVLFPELW 


HVRTTL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000010 Genomic DNA. Translation: AAU49146.1. Different initiation.
RefSeqYP_102169.1. NC_006348.1.

3D structure databases

HSSPHSSP built from PDB template 1YW0 based on UniProtKB Q8PDA8.
ProteinModelPortalQ62M99.
SMRQ62M99. Positions 37-306.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3091024.
GenomeReviewsGene locus BMA0351 in contig CP000010_GR.
KEGGbma:BMA0351.
PATRIC19115627. VBIBurMal55007_0352.
TIGRBMA0351.

Phylogenomic databases

HOGENOMHBG647485.
ProtClustDBCLSK2391472.

Enzyme and pathway databases

BioCycBMAL243160:BMA_0351-MONOMER.

Family and domain databases

InterProIPR017485. Trp_2-3-dOase_bac.
IPR004981. Trp_2_3_dOase.
[Graphical view]
KOK00453.
PANTHERPTHR10138. Trp_2_3_dOase. 1 hit.
PfamPF03301. Trp_dioxygenase. 1 hit.
[Graphical view]
TIGRFAMsTIGR03036. Trp_2_3_diox. 1 hit.
ProtoNetSearch...

Entry information

Entry nameT23O_BURMA
AccessionPrimary (citable) accession number: Q62M99
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: January 25, 2012
This is version 42 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families