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B4RUH2 (T23O_ALTMD) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 25. 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:MADE_1006210
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

Protein attributes

Sequence length362 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 – 362362Tryptophan 2,3-dioxygenase
PRO_0000360079

Regions

Region10 – 145Substrate binding By similarity
Region40 – 445Substrate binding By similarity

Sites

Metal binding2971Iron (heme axial ligand) By similarity
Binding site1111Substrate By similarity
Binding site1181Heme By similarity
Binding site3111Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4RUH2 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 955EDB34A2D407A2

FASTA36242,791
        10         20         30         40         50         60 
MKKNIEPCYY GDYLQLDKIL GAQDLQSEKY GDGAHEEMLF IIVHQVYELW FKQVLHELNA 

        70         80         90        100        110        120 
VIDTFNQEAV KDQQLTQVVH RLQRIIQIQK LMNDQIAIME TMTPQQFLSF RDYLVPASGF 

       130        140        150        160        170        180 
QSIQFKRLEI SLGLKREFRI DFDKQSFYNR LTDKDRALLE NLENKPSLFE LVDKWLSRMP 

       190        200        210        220        230        240 
LLKTEDFDFW QYYKDAADEM LKDDHHTVST SDMLSDTEKR QEIKDLQATM ENFDALFNET 

       250        260        270        280        290        300 
QFEKLRGEGK FRLSHNALLS ALFIKQYSEE PIFNLPFQLI TALTEIDEQL TIWRYRHAMM 

       310        320        330        340        350        360 
VQRMLGTKIG TGGSSGHHYL KKTTESNRIY LDFFNMATFL LPKSALPDLP ESVRRRLGFY 


LQ 

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed: 18670397] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001103 Genomic DNA. Translation: AEA97384.1.
RefSeqYP_004426382.1. NC_011138.2.

3D structure databases

ProteinModelPortalB4RUH2.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4RUH2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID10556583.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG647485.
OMAVPASGFQ.
ProtClustDBCLSK2307017.

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_ALTMD
AccessionPrimary (citable) accession number: B4RUH2
Secondary accession number(s): F2G4T0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: September 23, 2008
Last modified: December 14, 2011
This is version 25 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