T23O_TRICA
ID T23O_TRICA Reviewed; 388 AA.
AC Q95NN1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=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};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=GA-1, and GA-2;
RX PubMed=11805058; DOI=10.1093/genetics/160.1.225;
RA Lorenzen M.D., Brown S.J., Denell R.E., Beeman R.W.;
RT "Cloning and characterization of the Tribolium castaneum eye-color genes
RT encoding tryptophan oxygenase and kynurenine 3-monooxygenase.";
RL Genetics 160:225-234(2002).
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 (By similarity). Required for normal eye
CC pigmentation. {ECO:0000255|HAMAP-Rule:MF_03020,
CC ECO:0000269|PubMed:11805058}.
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; AY052390; AAL15464.1; -; mRNA.
DR EMBL; AY052392; AAL15466.1; -; Genomic_DNA.
DR RefSeq; NP_001034499.1; NM_001039410.1.
DR AlphaFoldDB; Q95NN1; -.
DR SMR; Q95NN1; -.
DR STRING; 7070.TC008028-PA; -.
DR GeneID; 654844; -.
DR KEGG; tca:654844; -.
DR CTD; 32026; -.
DR eggNOG; KOG3906; Eukaryota.
DR HOGENOM; CLU_045599_1_1_1; -.
DR OrthoDB; 896211at2759; -.
DR UniPathway; UPA00271; -.
DR UniPathway; UPA00333; UER00453.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase;
KW Tryptophan catabolism.
FT CHAIN 1..388
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000360886"
FT BINDING 54..58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT BINDING 309
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 324
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
SQ SEQUENCE 388 AA; 45423 MW; 96A34C73ED0F1F03 CRC64;
MSCPLRPSEA QEGDQLSEEC GMLYGEYLML DKILEAQRLL SEQNNQPVHD EHLFIVTHQA
YELWFKQIIY ELDSIRNIFS DVLEESQTLE ILKRLNRVVL ILKVLVDQVM ILETMTPLDF
MDFRCYLRPA SGFQSLQFRL LENKLGVRQE NRVKYNQNYS KVFGNDEKAL EQIAKSEKEP
SLTDLVQRWL ERTPGLELEG FNFWGKYQKA VEKLLTEQKE LAEKEEAETL KRYKLNDLEK
RREVYESIFK VEVHEALMSR GERRFSHKAL QGAIMITFYR DEPRFSQPHQ ILTLLMDIDS
LITKWRYNHV LMVQRMIGSS QLGTGGSSGY QYLRSTLSDR YKVFVDLFNL STFLIPRSYI
PPLSTSMRSH LCNWGSANST NIVSNGNN
