ID   T23O_XENTR              Reviewed;         406 AA.
AC   Q5EBG2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
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};
GN   Name=tdo2 {ECO:0000255|HAMAP-Rule:MF_03020};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; BC089667; AAH89667.1; -; mRNA.
DR   RefSeq; NP_001015733.1; NM_001015733.1.
DR   AlphaFoldDB; Q5EBG2; -.
DR   SMR; Q5EBG2; -.
DR   STRING; 8364.ENSXETP00000048482; -.
DR   PaxDb; Q5EBG2; -.
DR   DNASU; 548450; -.
DR   Ensembl; ENSXETT00000048482; ENSXETP00000048482; ENSXETG00000022396.
DR   GeneID; 548450; -.
DR   KEGG; xtr:548450; -.
DR   CTD; 6999; -.
DR   Xenbase; XB-GENE-976712; tdo2.
DR   eggNOG; KOG3906; Eukaryota.
DR   HOGENOM; CLU_045599_1_1_1; -.
DR   InParanoid; Q5EBG2; -.
DR   OMA; ERRHEHL; -.
DR   OrthoDB; 896211at2759; -.
DR   PhylomeDB; Q5EBG2; -.
DR   TreeFam; TF105827; -.
DR   Reactome; R-XTR-71240; Tryptophan catabolism.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000022396; Expressed in liver and 9 other tissues.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
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:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0019442; P:tryptophan catabolic process to acetyl-CoA; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW   Tryptophan catabolism.
FT   CHAIN           1..406
FT                   /note="Tryptophan 2,3-dioxygenase"
FT                   /id="PRO_0000247477"
FT   BINDING         72..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
FT   BINDING         328
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         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03020"
SQ   SEQUENCE   406 AA;  47700 MW;  EEF95FDF71884F8C CRC64;
     MSGCPFMGKK HHFNFSELSL EDKNEDSSQE GLNKASKGGL IYGDYLQLDK VLNAQELQSE
     KKGNKIHDEH LFIVTHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VVTRIHRISM
     ILKLLVEQFS VLETMTAMDF FDFRDYLSPA SGFQSLQFRL LENKIGVPEI LRVPYNRRHY
     RDNFKGETNE LLLKSEQELT LLGLVEAWLE RTPGLEEEGF HFWGKLEANI FRGLEEELQT
     VKTKPDSEEK EEQLAELQKQ KELFGALFDE RRHEHLLSKG ERRLSYKALK GALMIYFYRE
     EPRFQVPFQL LTSLMDIDTL MTKWRYNHVC MVHRMIGSKA GTGGSSGYQY LRSTVSDRYK
     VFVDLFNLST YLVPRHWVPR LNPSIHKFLY TAECCDSSYF SSDDSD