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P20351

- T23O_DROME

UniProt

P20351 - T23O_DROME

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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

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
Complete GO annotation...

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.
ExpressionAtlasiP20351. differential.

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

        10         20         30         40         50
MSCPYAGNGN DHDDSAVPLT TEVGKIYGEY LMLDKLLDAQ CMLSEEDKRP
60 70 80 90 100
VHDEHLFIIT HQAYELWFKQ IIFEFDSIRD MLDAEVIDET KTLEIVKRLN
110 120 130 140 150
RVVLILKLLV DQVPILETMT PLDFMDFRKY LAPASGFQSL QFRLIENKLG
160 170 180 190 200
VLTEQRVRYN QKYSDVFSDE EARNSIRNSE KDPSLLELVQ RWLERTPGLE
210 220 230 240 250
ESGFNFWAKF QESVDRFLEA QVQSAMEEPV EKAKNYRLMD IEKRREVYRS
260 270 280 290 300
IFDPAVHDAL VRRGDRRFSH RALQGAIMIT FYRDEPRFSQ PHQLLTLLMD
310 320 330 340 350
IDSLITKWRY NHVIMVQRMI GSQQLGTGGS SGYQYLRSTL SDRYKVFLDL
360 370
FNLSTFLIPR EAIPPLDETI RKKLINKSV
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.
ExpressionAtlasi P20351. differential.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 116 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