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P20351 (T23O_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptophan 2,3-dioxygenase

Short name=TDO
EC=1.13.11.11
Alternative name(s):
Protein vermilion
Tryptamin 2,3-dioxygenase
Tryptophan oxygenase
Short name=TO
Short name=TRPO
Tryptophan pyrrolase
Tryptophanase
Gene names
Name:v
ORF Names:CG5163
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring By similarity. Required during larval growth to control the level of potentially harmful free tryptophan in the hemolymph. In the adult the same reaction is the first step in the ommochrome biosynthetic pathway. Ref.1

Catalytic activity

L-tryptophan + O2 = N-formyl-L-kynurenine. HAMAP-Rule MF_03020

Cofactor

Binds 2 heme groups per tetramer By similarity. HAMAP-Rule MF_03020

Pathway

Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2. HAMAP-Rule MF_03020

Pigment biosynthesis; ommochrome biosynthesis. HAMAP-Rule MF_03020

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_03020

Developmental stage

High in late larvae and in adult. Ref.1

Sequence similarities

Belongs to the tryptophan 2,3-dioxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Tryptophan 2,3-dioxygenase HAMAP-Rule MF_03020
PRO_0000065780

Regions

Region27 – 315Substrate binding By similarity
Region57 – 615Substrate binding By similarity

Sites

Metal binding3121Iron (heme axial ligand) By similarity
Binding site1281Substrate By similarity
Binding site1351Heme By similarity
Binding site3271Substrate By similarity

Secondary structure

............................................... 379
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20351 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: E9E4C1B1C86D687F

FASTA37944,421
        10         20         30         40         50         60 
MSCPYAGNGN DHDDSAVPLT TEVGKIYGEY LMLDKLLDAQ CMLSEEDKRP VHDEHLFIIT 

        70         80         90        100        110        120 
HQAYELWFKQ IIFEFDSIRD MLDAEVIDET KTLEIVKRLN RVVLILKLLV DQVPILETMT 

       130        140        150        160        170        180 
PLDFMDFRKY LAPASGFQSL QFRLIENKLG VLTEQRVRYN QKYSDVFSDE EARNSIRNSE 

       190        200        210        220        230        240 
KDPSLLELVQ RWLERTPGLE ESGFNFWAKF QESVDRFLEA QVQSAMEEPV EKAKNYRLMD 

       250        260        270        280        290        300 
IEKRREVYRS IFDPAVHDAL VRRGDRRFSH RALQGAIMIT FYRDEPRFSQ PHQLLTLLMD 

       310        320        330        340        350        360 
IDSLITKWRY NHVIMVQRMI GSQQLGTGGS SGYQYLRSTL SDRYKVFLDL FNLSTFLIPR 

       370 
EAIPPLDETI RKKLINKSV 

« Hide

References

« Hide 'large scale' references
[1]"Structure and transcription of the Drosophila melanogaster vermilion gene and several mutant alleles."
Searles L.L., Ruth R.S., Pret A.-M., Fridell R.A., Ali A.J.
Mol. Cell. Biol. 10:1423-1431(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34147 Genomic DNA. Translation: AAA29014.1.
AE014298 Genomic DNA. Translation: AAF47978.1.
AY051478 mRNA. Translation: AAK92902.1.
PIRA34780.
RefSeqNP_511113.1. NM_078558.3.
UniGeneDm.7748.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4HKAX-ray2.70A24-379[»]
ProteinModelPortalP20351.
SMRP20351. Positions 24-368.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58442. 1 interaction.

Proteomic databases

PaxDbP20351.
PRIDEP20351.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0073386; FBpp0073242; FBgn0003965.
GeneID32026.
KEGGdme:Dmel_CG2155.
UCSCCG2155-RA. d. melanogaster.

Organism-specific databases

CTD32026.
FlyBaseFBgn0003965. v.

Phylogenomic databases

eggNOGCOG3483.
GeneTreeENSGT00390000008593.
InParanoidP20351.
KOK00453.
OMAYGEYLML.
OrthoDBEOG7MD4Q2.
PhylomeDBP20351.

Enzyme and pathway databases

BRENDA1.13.11.11. 1994.
UniPathwayUPA00271.
UPA00333; UER00453.

Gene expression databases

BgeeP20351.

Family and domain databases

HAMAPMF_01972. T23O.
InterProIPR004981. Trp_2_3_dOase.
[Graphical view]
PANTHERPTHR10138. PTHR10138. 1 hit.
PfamPF03301. Trp_dioxygenase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi32026.
NextBio776434.
PROP20351.

Entry information

Entry nameT23O_DROME
AccessionPrimary (citable) accession number: P20351
Secondary accession number(s): Q9VZ50
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase