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Q3JVD8 (T23O_BURP1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:BURPS1710b_1053
OrganismBurkholderia pseudomallei (strain 1710b) [Complete proteome] [HAMAP]
Taxonomic identifier320372 [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 ABA49981.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 306306Tryptophan 2,3-dioxygenase
PRO_0000360108

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
Q3JVD8 [UniParc].

Last modified January 20, 2009. Version 2.
Checksum: 2C27E8FCE42E6F7C

FASTA30634,813
        10         20         30         40         50         60 
MQPPGDDAAP RCPFAGAHAP DAPHVPEAAG DDAQAGWHRA 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 RHDRTVEAAW LAVYREPNAH 

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


HVRTTL 

« Hide

References

[1]Woods D.E., Nierman W.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1710b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000124 Genomic DNA. Translation: ABA49981.1. Different initiation.
RefSeqYP_332465.1. NC_007434.1.

3D structure databases

ProteinModelPortalQ3JVD8.
SMRQ3JVD8. Positions 46-306.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3JVD8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3689313.
GenomeReviewsGene locus BURPS1710b_1053 in contig CP000124_GR.
KEGGbpm:BURPS1710b_1053.
PATRIC19234350. VBIBurPse115837_1064.
TIGRBURPS1710b_1053.

Phylogenomic databases

eggNOGCOG3483.
HOGENOMHBG647485.
ProtClustDBCLSK2391472.

Enzyme and pathway databases

BioCycBPSE320372:BURPS1710B_A1106-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_BURP1
AccessionPrimary (citable) accession number: Q3JVD8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: January 25, 2012
This is version 39 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