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P20351

- T23O_DROME

UniProt

P20351 - T23O_DROME

Protein

Tryptophan 2,3-dioxygenase

Gene

v

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    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.1 PublicationUniRule annotation

    Catalytic activityi

    L-tryptophan + O2 = N-formyl-L-kynurenine.UniRule annotation

    Cofactori

    Binds 2 heme groups per tetramer.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei128 – 1281SubstrateUniRule annotation
    Binding sitei135 – 1351HemeUniRule annotation
    Metal bindingi312 – 3121Iron (heme axial ligand)UniRule annotation
    Binding sitei327 – 3271SubstrateUniRule annotation

    GO - Molecular functioni

    1. heme binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. tryptophan 2,3-dioxygenase activity Source: UniProtKB

    GO - Biological processi

    1. compound eye pigmentation Source: FlyBase
    2. kynurenine metabolic process Source: FlyBase
    3. ommochrome biosynthetic process Source: FlyBase
    4. positive regulation of neuron death Source: FlyBase
    5. tryptophan catabolic process Source: FlyBase
    6. tryptophan catabolic process to acetyl-CoA Source: RefGenome
    7. tryptophan catabolic process to kynurenine Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Tryptophan catabolism

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.13.11.11. 1994.
    ReactomeiREACT_205738. Tryptophan catabolism.
    UniPathwayiUPA00271.
    UPA00333; UER00453.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tryptophan 2,3-dioxygenaseUniRule annotation (EC:1.13.11.11UniRule annotation)
    Short name:
    TDOUniRule annotation
    Alternative name(s):
    Protein vermilionUniRule annotation
    Tryptamin 2,3-dioxygenaseUniRule annotation
    Tryptophan oxygenaseUniRule annotation
    Short name:
    TOUniRule annotation
    Short name:
    TRPOUniRule annotation
    Tryptophan pyrrolaseUniRule annotation
    TryptophanaseUniRule annotation
    Gene namesi
    Name:vUniRule annotation
    ORF Names:CG5163
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0003965. v.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 379379Tryptophan 2,3-dioxygenasePRO_0000065780Add
    BLAST

    Proteomic databases

    PaxDbiP20351.
    PRIDEiP20351.

    Expressioni

    Developmental stagei

    High in late larvae and in adult.1 Publication

    Gene expression databases

    BgeeiP20351.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    BioGridi58442. 1 interaction.

    Structurei

    Secondary structure

    1
    379
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 304
    Helixi33 – 364
    Helixi43 – 464
    Helixi54 – 8229
    Beta strandi83 – 853
    Helixi89 – 11628
    Helixi121 – 1255
    Helixi128 – 1303
    Helixi135 – 1373
    Helixi140 – 14910
    Helixi153 – 1553
    Helixi163 – 1664
    Helixi170 – 18112
    Helixi185 – 19410
    Turni201 – 2044
    Helixi206 – 22621
    Helixi231 – 25222
    Helixi254 – 2629
    Helixi270 – 28112
    Helixi286 – 32035
    Helixi331 – 3388
    Helixi348 – 3514
    Helixi352 – 3565
    Helixi360 – 3623

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HKAX-ray2.70A24-379[»]
    ProteinModelPortaliP20351.
    SMRiP20351. Positions 24-368.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 315Substrate bindingUniRule annotation
    Regioni57 – 615Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the tryptophan 2,3-dioxygenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3483.
    GeneTreeiENSGT00390000008593.
    InParanoidiP20351.
    KOiK00453.
    OMAiYGEYLML.
    OrthoDBiEOG7MD4Q2.
    PhylomeDBiP20351.

    Family and domain databases

    HAMAPiMF_01972. T23O.
    InterProiIPR004981. Trp_2_3_dOase.
    [Graphical view]
    PANTHERiPTHR10138. PTHR10138. 1 hit.
    PfamiPF03301. Trp_dioxygenase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P20351-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSCPYAGNGN DHDDSAVPLT TEVGKIYGEY LMLDKLLDAQ CMLSEEDKRP    50
    VHDEHLFIIT HQAYELWFKQ IIFEFDSIRD MLDAEVIDET KTLEIVKRLN 100
    RVVLILKLLV DQVPILETMT PLDFMDFRKY LAPASGFQSL QFRLIENKLG 150
    VLTEQRVRYN QKYSDVFSDE EARNSIRNSE KDPSLLELVQ RWLERTPGLE 200
    ESGFNFWAKF QESVDRFLEA QVQSAMEEPV EKAKNYRLMD IEKRREVYRS 250
    IFDPAVHDAL VRRGDRRFSH RALQGAIMIT FYRDEPRFSQ PHQLLTLLMD 300
    IDSLITKWRY NHVIMVQRMI GSQQLGTGGS SGYQYLRSTL SDRYKVFLDL 350
    FNLSTFLIPR EAIPPLDETI RKKLINKSV 379
    Length:379
    Mass (Da):44,421
    Last modified:February 1, 1991 - v1
    Checksum:iE9E4C1B1C86D687F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34147 Genomic DNA. Translation: AAA29014.1.
    AE014298 Genomic DNA. Translation: AAF47978.1.
    AY051478 mRNA. Translation: AAK92902.1.
    PIRiA34780.
    RefSeqiNP_511113.1. NM_078558.3.
    UniGeneiDm.7748.

    Genome annotation databases

    EnsemblMetazoaiFBtr0073386; FBpp0073242; FBgn0003965.
    GeneIDi32026.
    KEGGidme:Dmel_CG2155.
    UCSCiCG2155-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34147 Genomic DNA. Translation: AAA29014.1 .
    AE014298 Genomic DNA. Translation: AAF47978.1 .
    AY051478 mRNA. Translation: AAK92902.1 .
    PIRi A34780.
    RefSeqi NP_511113.1. NM_078558.3.
    UniGenei Dm.7748.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HKA X-ray 2.70 A 24-379 [» ]
    ProteinModelPortali P20351.
    SMRi P20351. Positions 24-368.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58442. 1 interaction.

    Proteomic databases

    PaxDbi P20351.
    PRIDEi P20351.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0073386 ; FBpp0073242 ; FBgn0003965 .
    GeneIDi 32026.
    KEGGi dme:Dmel_CG2155.
    UCSCi CG2155-RA. d. melanogaster.

    Organism-specific databases

    CTDi 32026.
    FlyBasei FBgn0003965. v.

    Phylogenomic databases

    eggNOGi COG3483.
    GeneTreei ENSGT00390000008593.
    InParanoidi P20351.
    KOi K00453.
    OMAi YGEYLML.
    OrthoDBi EOG7MD4Q2.
    PhylomeDBi P20351.

    Enzyme and pathway databases

    UniPathwayi UPA00271 .
    UPA00333 ; UER00453 .
    BRENDAi 1.13.11.11. 1994.
    Reactomei REACT_205738. Tryptophan catabolism.

    Miscellaneous databases

    GenomeRNAii 32026.
    NextBioi 776434.
    PROi P20351.

    Gene expression databases

    Bgeei P20351.

    Family and domain databases

    HAMAPi MF_01972. T23O.
    InterProi IPR004981. Trp_2_3_dOase.
    [Graphical view ]
    PANTHERi PTHR10138. PTHR10138. 1 hit.
    Pfami PF03301. Trp_dioxygenase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.

    Entry informationi

    Entry nameiT23O_DROME
    AccessioniPrimary (citable) accession number: P20351
    Secondary accession number(s): Q9VZ50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3