Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A9AGH1 (T23O_BURM1)

Last modified June 16, 2009. Version 13. 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: Bmul_0718, BMULJ_02542
OrganismBurkholderia multivorans (strain ATCC 17616 / 249) [Complete proteome] [HAMAP]
Taxonomic identifier395019 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length310 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 – 310310Tryptophan 2,3-dioxygenase
PRO_0000360102

Regions

Region54 – 585Substrate binding By similarity
Region79 – 835Substrate binding By similarity

Sites

Metal binding2681Iron (heme axial ligand) By similarity
Binding site1411Substrate By similarity
Binding site1451Substrate By similarity
Binding site1521Heme By similarity
Binding site2821Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A9AGH1-1 [UniParc].

Last modified January 20, 2009. Version 2.
Checksum: 9064E432AAB811FB

FASTA31035,343
        10         20         30         40         50         60 
MQPPGNDAPA GCPFSGARAQ GTQAAHEAPH VPGDAGEQAG WHNAQLDFSK SMSYGDYLSL 

        70         80         90        100        110        120 
NAILNAQHPL SPDHNEMLFI IQHQTSELWM KLALFELRGA LDAVRSDALP PAFKMLARVS 

       130        140        150        160        170        180 
RILEQLVQAW NVLSTMTPSE YSAMRPYLGQ SSGFQSYQYR QLEFLLGNKN AQMLQPHAHR 

       190        200        210        220        230        240 
PDILEQVRAT LDAPSFYDEV VRLLARRGFP IAPSRLDRDW RQPTQHDETV EAAWLEVYRH 

       250        260        270        280        290        300 
PQQHWELYEM AEELVDLEDA FRQWRFRHVT TVERIIGFKQ GTGGTSGAPY LRKMLDVVLF 

       310 
PELWHVRTTL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia multivorans ATCC 17616."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Complete genome sequence of Burkholderia multivorans ATCC 17616."
Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000868 Genomic DNA. Translation: ABX14413.1. Different initiation.
AP009385 Genomic DNA. Translation: BAG44433.1.
RefSeqYP_001578910.1.
YP_001946969.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5767643.
6359606.
GenomeReviewsGene locus BMULJ_02542 in contig AP009385_GR.
Gene locus Bmul_0718 in contig CP000868_GR.
KEGGbmj:BMULJ_02542.
bmu:Bmul_0718.

Organism-specific databases

CMRSearch...

Family and domain databases

InterProIPR017485. Trp_2-3-dOase_bac.
IPR004981. Trp_2_3_dOase.
[Graphical view]
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_BURM1
AccessionPrimary (citable) accession number: A9AGH1
Secondary accession number(s): B3D321
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: June 16, 2009
This is version 13 of the entry and version 2 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