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Protein

Tryptophan 2,3-dioxygenase

Gene

v

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety (PubMed:23333332). 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 (PubMed:2108317).1 PublicationUniRule annotation1 Publication

Catalytic activityi

L-tryptophan + O2 = N-formyl-L-kynurenine.UniRule annotation1 Publication

Cofactori

hemeUniRule annotation1 PublicationNote: Binds 1 heme group per subunit.UniRule annotation1 Publication

Pathwayi: L-tryptophan degradation via kynurenine pathway

This protein is involved in step 1 of the subpathway that synthesizes L-kynurenine from L-tryptophan.UniRule annotation1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Tryptophan 2,3-dioxygenase (v)
  2. Kynurenine formamidase (KFase), Kynurenine formamidase (KFase)
This subpathway is part of the pathway L-tryptophan degradation via kynurenine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-kynurenine from L-tryptophan, the pathway L-tryptophan degradation via kynurenine pathway and in Amino-acid degradation.

Pathwayi: ommochrome biosynthesis

This protein is involved in the pathway ommochrome biosynthesis, which is part of Pigment biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway ommochrome biosynthesis and in Pigment biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei128SubstrateUniRule annotation1
Metal bindingi312Iron (heme axial ligand)UniRule annotationCombined sources1 Publication1
Binding sitei327SubstrateUniRule annotation1

GO - Molecular functioni

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

GO - Biological processi

  • compound eye pigmentation Source: FlyBase
  • kynurenine metabolic process Source: FlyBase
  • ommochrome biosynthetic process Source: FlyBase
  • positive regulation of neuron death Source: FlyBase
  • protein homotetramerization Source: UniProtKB
  • tryptophan catabolic process Source: FlyBase
  • tryptophan catabolic process to acetyl-CoA Source: GO_Central
  • tryptophan catabolic process to kynurenine Source: UniProtKB

Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processTryptophan catabolism
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.11 1994
ReactomeiR-DME-71240 Tryptophan catabolism
UniPathwayiUPA00271
UPA00333; UER00453

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan 2,3-dioxygenaseUniRule annotation (EC:1.13.11.11UniRule annotation1 Publication)
Short name:
TDOUniRule annotation
Alternative name(s):
Protein vermilion1 PublicationUniRule 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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003965 v

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi123D → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi236Y → F: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi309R → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi335Y → F: Strongly reduced enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000657801 – 379Tryptophan 2,3-dioxygenaseAdd BLAST379

Proteomic databases

PaxDbiP20351
PRIDEiP20351

Expressioni

Developmental stagei

High in late larvae and in adult.1 Publication

Gene expression databases

BgeeiFBgn0003965
ExpressionAtlasiP20351 baseline and differential
GenevisibleiP20351 DM

Interactioni

Subunit structurei

Homotetramer. Dimer of dimers.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi58442, 2 interactors
STRINGi7227.FBpp0073242

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 30Combined sources4
Helixi33 – 36Combined sources4
Helixi43 – 46Combined sources4
Helixi54 – 82Combined sources29
Beta strandi83 – 85Combined sources3
Helixi89 – 116Combined sources28
Helixi121 – 125Combined sources5
Helixi128 – 130Combined sources3
Helixi135 – 137Combined sources3
Helixi140 – 149Combined sources10
Helixi153 – 155Combined sources3
Helixi163 – 166Combined sources4
Helixi170 – 181Combined sources12
Helixi185 – 194Combined sources10
Turni201 – 204Combined sources4
Helixi206 – 226Combined sources21
Helixi231 – 252Combined sources22
Helixi254 – 262Combined sources9
Helixi270 – 281Combined sources12
Helixi286 – 320Combined sources35
Helixi331 – 338Combined sources8
Helixi348 – 351Combined sources4
Helixi352 – 356Combined sources5
Helixi360 – 362Combined sources3

3D structure databases

ProteinModelPortaliP20351
SMRiP20351
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni57 – 61Substrate bindingUniRule annotation5

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3906 Eukaryota
COG3483 LUCA
InParanoidiP20351
KOiK00453
OMAiYWDLYQL
OrthoDBiEOG091G080K
PhylomeDBiP20351

Family and domain databases

HAMAPiMF_01972 T23O, 1 hit
InterProiView protein in InterPro
IPR037217 Trp/Indoleamine_2_3_dOase-like
IPR004981 Trp_2_3_dOase
PANTHERiPTHR10138 PTHR10138, 1 hit
PfamiView protein in Pfam
PF03301 Trp_dioxygenase, 1 hit
SUPFAMiSSF140959 SSF140959, 2 hits

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:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiT23O_DROME
AccessioniPrimary (citable) accession number: P20351
Secondary accession number(s): Q9VZ50
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 23, 2018
This is version 141 of the entry and version 1 of the sequence. See 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

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