ID   T23O_DROGR              Reviewed;         377 AA.
AC   B4JKK1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=GH12679;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00;
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH916370; EDW00104.1; -; Genomic_DNA.
DR   RefSeq; XP_001991479.1; XM_001991443.1.
DR   AlphaFoldDB; B4JKK1; -.
DR   SMR; B4JKK1; -.
DR   STRING; 7222.FBpp0146585; -.
DR   PRIDE; B4JKK1; -.
DR   EnsemblMetazoa; FBtr0148093; FBpp0146585; FBgn0120158.
DR   GeneID; 6564497; -.
DR   KEGG; dgr:6564497; -.
DR   eggNOG; KOG3906; Eukaryota.
DR   HOGENOM; CLU_045599_1_1_1; -.
DR   InParanoid; B4JKK1; -.
DR   OMA; WRWRNDH; -.
DR   OrthoDB; 896211at2759; -.
DR   PhylomeDB; B4JKK1; -.
DR   UniPathway; UPA00271; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000001070; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0006727; P:ommochrome biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; ISS:UniProtKB.
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; PTHR10138; 1.
DR   Pfam; PF03301; Trp_dioxygenase; 1.
DR   SUPFAM; SSF140959; SSF140959; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW   Tryptophan catabolism.
FT   CHAIN           1..377
FT                   /note="Tryptophan 2,3-dioxygenase"
FT                   /id="PRO_0000360876"
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   377 AA;  43939 MW;  85054B06A5729877 CRC64;
     MSCPYAGNSN EHDDAAVPLS NDVGKIYGEY LMLDKLLDAQ CMLSMEDKRP VHDEHLFIIT
     HQAYELWFKQ IIFEFDSIRD MLDAEVIDET KTLEIVKRLN RVVLILKLLV DQVPILETMT
     PLDFMDFRKY LAPASGFQSL QFRLIENKLG VLTEQRVKYN QKYSDVFGND ERALNAIRSS
     EDNPSLLELV QRWLERTPGL EADGFNFWEK FQHSVDQFLA AQVHSALLEP VEQAKNYRLM
     DIEKRREVYR SIFDPALHEA LVKRGDRRFS HGALQGAIMI TFYRDEPRFS QPHQLLTLLM
     DIDSLITKWR YNHVIMVQRM IGSQQLGTGG SSGYQYLRST LSDRYKVFLD LFNLSTFLIP
     REAIPPLDES IRQKLIH