ID   T23O_DROWI              Reviewed;         380 AA.
AC   B4MSH7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE            Short=TDO {ECO:0000255|HAMAP-Rule:MF_03020};
DE            EC=1.13.11.11 {ECO:0000255|HAMAP-Rule:MF_03020};
DE   AltName: Full=Protein vermilion {ECO:0000255|HAMAP-Rule:MF_03020};
DE   AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE   AltName: Full=Tryptophan oxygenase {ECO:0000255|HAMAP-Rule:MF_03020};
DE            Short=TO {ECO:0000255|HAMAP-Rule:MF_03020};
DE            Short=TRPO {ECO:0000255|HAMAP-Rule:MF_03020};
DE   AltName: Full=Tryptophan pyrrolase {ECO:0000255|HAMAP-Rule:MF_03020};
DE   AltName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_03020};
GN   Name=v {ECO:0000255|HAMAP-Rule:MF_03020}; ORFNames=GK19977;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Heme-dependent dioxygenase that catalyzes the oxidative
CC       cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-
CC       tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage
CC       of the indole moiety. {ECO:0000255|HAMAP-Rule:MF_03020}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tryptophan + O2 = N-formyl-L-kynurenine;
CC         Xref=Rhea:RHEA:24536, ChEBI:CHEBI:15379, ChEBI:CHEBI:57912,
CC         ChEBI:CHEBI:58629; EC=1.13.11.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03020};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03020};
CC       Note=Binds 1 heme group per subunit. {ECO:0000255|HAMAP-Rule:MF_03020};
CC   -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
CC       kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_03020}.
CC   -!- PATHWAY: Pigment biosynthesis; ommochrome biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03020}.
CC   -!- SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_03020}.
CC   -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03020}.
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DR   EMBL; CH963851; EDW75066.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4MSH7; -.
DR   SMR; B4MSH7; -.
DR   STRING; 7260.B4MSH7; -.
DR   EnsemblMetazoa; XM_002064044.4; XP_002064080.1; LOC6641329.
DR   GeneID; 6641329; -.
DR   KEGG; dwi:6641329; -.
DR   CTD; 136040130; -.
DR   eggNOG; KOG3906; Eukaryota.
DR   HOGENOM; CLU_045599_1_1_1; -.
DR   OMA; WRWRNDH; -.
DR   OrthoDB; 447477at2759; -.
DR   PhylomeDB; B4MSH7; -.
DR   UniPathway; UPA00271; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0004833; F:L-tryptophan 2,3-dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006569; P:L-tryptophan catabolic process; ISS:UniProtKB.
DR   GO; GO:0006727; P:ommochrome biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:EnsemblMetazoa.
DR   FunFam; 1.10.287.3810:FF:000001; Tryptophan 2,3-dioxygenase; 1.
DR   Gene3D; 1.10.287.3810; -; 1.
DR   Gene3D; 1.20.58.480; -; 1.
DR   HAMAP; MF_01972; T23O; 1.
DR   InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR   InterPro; IPR004981; Trp_2_3_dOase.
DR   PANTHER; PTHR10138; TRYPTOPHAN 2,3-DIOXYGENASE; 1.
DR   PANTHER; PTHR10138:SF0; TRYPTOPHAN 2,3-DIOXYGENASE; 1.
DR   Pfam; PF03301; Trp_dioxygenase; 1.
DR   SUPFAM; SSF140959; Indolic compounds 2,3-dioxygenase-like; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW   Tryptophan catabolism.
FT   CHAIN           1..380
FT                   /note="Tryptophan 2,3-dioxygenase"
FT                   /id="PRO_0000360883"
FT   BINDING         57..61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT   BINDING         313
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
SQ   SEQUENCE   380 AA;  44405 MW;  FDE68A1CA8CEC99A CRC64;
     MSCPYAGNGN EHDDSAVPLS NEIGKIYGEY LMLDKVLDAQ CMLSKEDKRP VHDEHLFIIT
     HQAYELWFKQ IIFEFDSIRD MLNAEVIDET KTLEIVKRLN RVVLILKLLV DQVPILETMT
     PLDFMDFRKY LAPASGFQSM QFRLIENKLG VLTEQRVKYN QKYSDVFGND AQALNAIRNS
     EIEPSLLELV QRWLERTPGL EEDGFNFWQK FQQSVDQFLD AQVQSAMEEP VEQAKNYRLM
     DIEKRREVYR SIFDTAVHEA LVKRGDRRFS HRALQGAIMI TFYRDEPRFS QPHQLLTLLM
     DIDSLITKWR YNHVIMVQRM IGSQQLGTGG SSGYQYLRST LSDRYKVFLD LFNLSTFLIP
     REAIPPLDES IRKKLINKSV
//