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A3MHE1 (T23O_BURM7) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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:BMA10247_0098
OrganismBurkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]
Taxonomic identifier320389 [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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 306306Tryptophan 2,3-dioxygenase
PRO_0000360103

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
A3MHE1 [UniParc].

Last modified April 3, 2007. Version 1.
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 

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References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10247.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000548 Genomic DNA. Translation: ABO06394.1.
RefSeqYP_001079677.1. NC_009080.1.

3D structure databases

ProteinModelPortalA3MHE1.
SMRA3MHE1. Positions 37-306.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3MHE1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4892910.
GenomeReviewsGene locus BMA10247_0098 in contig CP000548_GR.
KEGGbmn:BMA10247_0098.
PATRIC19142601. VBIBurMal96640_2367.
TIGRBMA10247_0098.

Phylogenomic databases

HOGENOMHBG647485.
OMAQYREIEF.
ProtClustDBCLSK2391472.

Enzyme and pathway databases

BioCycBMAL320389:BMA10247_0098-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_BURM7
AccessionPrimary (citable) accession number: A3MHE1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: April 3, 2007
Last modified: December 14, 2011
This is version 36 of the entry and version 1 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