T23O_DROVI
ID T23O_DROVI Reviewed; 380 AA.
AC B4M818;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 62.
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=GJ16721;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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 -!- SEQUENCE CAUTION:
CC Sequence=EDW62294.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CH940653; EDW62294.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_002056808.2; XM_002056772.2.
DR AlphaFoldDB; B4M818; -.
DR SMR; B4M818; -.
DR STRING; 7244.FBpp0231138; -.
DR GeneID; 6633596; -.
DR KEGG; dvi:6633596; -.
DR eggNOG; KOG3906; Eukaryota.
DR InParanoid; B4M818; -.
DR UniPathway; UPA00271; -.
DR UniPathway; UPA00333; UER00453.
DR Proteomes; UP000008792; 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..380
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000360882"
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; 44357 MW; 2CCE428FA8511436 CRC64;
MSCPYAGNGN EHDDGAVPLS NEVGKIYGEY LMLDKLLDAQ CMLSMEDKRP VHDEHLFIIT
HQAYELWFKQ IIFEFDSIRV MLDEEVIDET KTLEIVKRLN RVVLILKLLV DQVPILETMT
PLDFMDFRKY LAPASGFQSL QFRLIENKLG VLTEQRVKYN QKYSDVFGND ERALHAIRSS
EDGPSLLVLV QRWLERTPGL EEEGFNFWSK FQQSVDQFLA AQVQSALLEP VEWAKNYRLM
DIEKRREVYR SIFDPAVHEA LVKRGDRRFS HRALQGAIMI TFYRDEPRFS QPHQLLTLLM
DIDSLITKWR YNHVIMVQRM IGSQQLGTGG SSGYQYLRST LSDRYKVFLD LFNLSTFLIP
REAIPPLDET IRKKLVHKSV
