T23O_DROAN
ID T23O_DROAN Reviewed; 380 AA.
AC B3MQP7; O17440;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=GF20476;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9576938; DOI=10.1073/pnas.95.10.5649;
RA Stephan W., Xing L., Kirby D.A., Braverman J.M.;
RT "A test of the background selection hypothesis based on nucleotide data
RT from Drosophila ananassae.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:5649-5654(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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}.
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DR EMBL; AF028834; AAC24239.1; -; Genomic_DNA.
DR EMBL; CH902621; EDV44673.1; -; Genomic_DNA.
DR RefSeq; XP_001963597.1; XM_001963561.2.
DR AlphaFoldDB; B3MQP7; -.
DR SMR; B3MQP7; -.
DR STRING; 7217.FBpp0123668; -.
DR EnsemblMetazoa; FBtr0125176; FBpp0123668; FBgn0014630.
DR GeneID; 6508747; -.
DR KEGG; dan:6508747; -.
DR eggNOG; KOG3906; Eukaryota.
DR HOGENOM; CLU_045599_1_1_1; -.
DR InParanoid; B3MQP7; -.
DR OMA; WRWRNDH; -.
DR OrthoDB; 896211at2759; -.
DR PhylomeDB; B3MQP7; -.
DR UniPathway; UPA00271; -.
DR UniPathway; UPA00333; UER00453.
DR Proteomes; UP000007801; 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:1901216; P:positive regulation of neuron death; IEA:EnsemblMetazoa.
DR GO; GO:0051289; P:protein homotetramerization; IEA:EnsemblMetazoa.
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..380
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000360874"
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"
FT CONFLICT 379
FT /note="S -> N (in Ref. 1; AAC24239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 44343 MW; 535B078B1B52C226 CRC64;
MSCPYAGSGN DHDDAAVPLS TEVGKIYGEY LMLDKLLDAQ CMLSKEDKRP VHDEHLFIIT
HQAYELWFKQ IIFEFDSIRD MLDAEVIDET KTLEIVKRLN RVVLILKLLV DQVPILETMT
PLDFMDFRKY LAPASGFQSL QFRLIENKLG VLTEQRVRYN QKYSDVFGGD EDALTAIRSS
EQEPSLLELV QRWLERTPGL EESGFNFWEK FQQSVDKFLE AQVHSAMEEP VERAKNYRLM
DIEKRREVYR SIFDPAVHDA LVRRGDRRFS HRALQGAIMI TFYRDEPRFS QPHQLLTLLM
DIDSLITKWR YNHVIMVQRM IGSQQLGTGG SSGYQYLRST LSDRYKVFLD LFNLSTFLIP
REAIPPLDES IRKKLINKSV
