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Reviewed, UniProtKB/Swiss-Prot Q2N5X1 (T23O_ERYLH)

Last modified November 3, 2009. Version 21. 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: ELI_14140
OrganismErythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]
Taxonomic identifier314225 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesErythrobacteraceaeErythrobacter

Protein attributes

Sequence length263 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 – 263263Tryptophan 2,3-dioxygenase
PRO_0000360114

Regions

Region7 – 115Substrate binding By similarity
Region32 – 365Substrate binding By similarity

Sites

Metal binding2211Iron (heme axial ligand) By similarity
Binding site941Substrate By similarity
Binding site981Substrate By similarity
Binding site1051Heme By similarity
Binding site2351Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2N5X1-1 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 35222157E9DEDA18

FASTA26330,341
        10         20         30         40         50         60 
MAQDVTYSSY LDLDRILAAQ HPVSGAHDEM LFIIVHQASE LWLKLCLHEL FAARDCIAAD 

        70         80         90        100        110        120 
NLRPSFKMLS RVARAQTQLI QSWDVLSTMT PHDYSQIRPH LGRSSGFQSP QYRMMEFLLG 

       130        140        150        160        170        180 
GRNPDMVAMH EPTPEIATAL REELARTSLY DEAIRLLSRR GFAIPDEVLA RKLDEVWVRS 

       190        200        210        220        230        240 
EEVEAAWAEI YRDPQQHWDL YELAEKLVDL EYHFQRWRFG HLKTVERIIG FKRGTGGTKG 

       250        260 
VPYLEGVLKQ AFFPELLSVR TAI 

« Hide

References

[1]Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravits S., Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000157 Genomic DNA. Translation: ABC64920.1.
RefSeqYP_459717.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2N5X1.

Genome annotation databases

GeneID3871638.
GenomeReviewsGene locus ELI_14140 in contig CP000157_GR.
KEGGeli:ELI_14140.
NMPDRfig|314225.3.peg.190.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMKLILHE.

Enzyme and pathway databases

BioCycELIT314225:ELI_14140-MON.

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_ERYLH
AccessionPrimary (citable) accession number: Q2N5X1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: February 7, 2006
Last modified: November 3, 2009
This is version 21 of the entry and version 1 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