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P48776 (T23O_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:Tdo2
Synonyms:Tdo
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Incorporates oxygen into the indole moiety of tryptophan. Has a broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin 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.

Ontologies

Keywords
   Biological processTryptophan catabolism
   DomainCoiled coil
   LigandHeme
Iron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtryptophan catabolic process to kynurenine

Inferred from electronic annotation. Source: InterPro

   Molecular functiontryptophan 2,3-dioxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Tryptophan 2,3-dioxygenase
PRO_0000072400

Regions

Region42 – 465Substrate binding By similarity
Region72 – 765Substrate binding By similarity
Coiled coil229 – 26840 Potential

Sites

Metal binding3281Iron (heme axial ligand) By similarity
Binding site1441Substrate By similarity
Binding site1511Heme By similarity
Binding site3421Substrate By similarity

Amino acid modifications

Modified residue191Phosphoserine Ref.3
Modified residue1551Phosphoserine By similarity

Experimental info

Sequence conflict181V → L in AAB60491. Ref.1
Sequence conflict2291N → K in AAB60491. Ref.1
Sequence conflict2401R → K in AAB60491. Ref.1
Sequence conflict2451T → K in AAB60491. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48776 [UniParc].

Last modified January 20, 2009. Version 2.
Checksum: 201835A021BE7A24

FASTA40647,756
        10         20         30         40         50         60 
MSGCPFAGNS VGYTLKNVSM EDNEEDRAQT GVNRASKGGL IYGNYLQLEK ILNAQELQSE 

        70         80         90        100        110        120 
VKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VIARMHRVVV 

       130        140        150        160        170        180 
IFKLLVQQFS VLETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQS LRVPYNRKHY 

       190        200        210        220        230        240 
RDNFGGDYNE LLLKSEQEQT LLQLVEAWLE RTPGLEPNGF NFWGKFEKNI LKGLEEEFLR 

       250        260        270        280        290        300 
IQAKTDSEEK EEQMAEFRKQ KEVLLCLFDE KRHDYLLSKG ERRLSYRALQ GALMIYFYRE 

       310        320        330        340        350        360 
EPRFQVPFQL LTSLMDIDTL MTKWRYNHVC MVHRMLGTKA GTGGSSGYHY LRSTVSDRYK 

       370        380        390        400 
VFVDLFNLST YLVPRHWVPK MNPIIHKFLY TAEYSDSSYF SSDESD

« Hide

References

« Hide 'large scale' references
[1]Novoradovsky A., Goldman D.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: DBA/2J.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U24493 mRNA. Translation: AAB60491.1.
AC159260 Genomic DNA. No translation available.
IPIIPI00114381.
RefSeqNP_064295.2. NM_019911.2.
UniGeneMm.258622.

3D structure databases

ProteinModelPortalP48776.
SMRP48776. Positions 26-372.
ModBaseSearch...

Protein-protein interaction databases

STRINGP48776.

PTM databases

PhosphoSiteP48776.

Proteomic databases

PRIDEP48776.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029645; ENSMUSP00000029645; ENSMUSG00000028011.
GeneID56720.
KEGGmmu:56720.

Organism-specific databases

CTD6999.
MGIMGI:1928486. Tdo2.

Phylogenomic databases

eggNOGroNOG12771.
HOGENOMHBG647485.
HOVERGENHBG003043.
InParanoidP48776.
OMAKLLVDQV.
OrthoDBEOG4933J4.
PhylomeDBP48776.

Enzyme and pathway databases

BRENDA1.13.11.11. 3474.

Gene expression databases

ArrayExpressP48776.
BgeeP48776.
CleanExMM_TDO2.
GenevestigatorP48776.
GermOnlineENSMUSG00000028011. Mus musculus.

Family and domain databases

InterProIPR004981. Trp_2_3_dOase.
[Graphical view]
KOK00453.
PANTHERPTHR10138. Trp_2_3_dOase. 1 hit.
PfamPF03301. Trp_dioxygenase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameT23O_MOUSE
AccessionPrimary (citable) accession number: P48776
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 20, 2009
Last modified: November 16, 2011
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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