ID   T23O_CAEEL              Reviewed;         403 AA.
AC   Q09474;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Tryptophan 2,3-dioxygenase;
DE            Short=TDO;
DE            EC=1.13.11.11;
DE   AltName: Full=Tryptophan pyrrolase;
DE            Short=Tryptophanase;
DE   AltName: Full=Tryptophan oxygenase;
DE            Short=TRPO;
DE            Short=TO;
DE   AltName: Full=Tryptamin 2,3-dioxygenase;
GN   ORFNames=C28H8.11;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalyzes the oxidative cleavage of the L-tryptophan (L-
CC       Trp) pyrrole ring (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-tryptophan + O(2) = N-formyl-L-kynurenine.
CC   -!- COFACTOR: Binds 2 heme groups per tetramer (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
CC       kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-316265, EBI-316265;
CC       O62107:gale-1; NbExp=1; IntAct=EBI-316265, EBI-316270;
CC       O61899:kel-8; NbExp=1; IntAct=EBI-316265, EBI-312469;
CC   -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
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DR   EMBL; U20861; AAA62299.1; -; Genomic_DNA.
DR   PIR; B88470; B88470.
DR   RefSeq; NP_498284.1; -.
DR   UniGene; Cel.10783; -.
DR   DIP; DIP:26438N; -.
DR   IntAct; Q09474; 3.
DR   PRIDE; Q09474; -.
DR   Ensembl; C28H8.11; Caenorhabditis elegans.
DR   GeneID; 175836; -.
DR   NMPDR; fig|6239.3.peg.9980; -.
DR   WormBase; WBGene00016201; C28H8.11.
DR   WormPep; C28H8.11; CE01822.
DR   OMA; Q09474; HYRDNFR.
DR   BRENDA; 1.13.11.11; 672.
DR   NextBio; 889870; -.
DR   ArrayExpress; Q09474; -.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR   InterPro; IPR004981; Trp_2_3_dOase.
DR   PANTHER; PTHR10138; Trp_2_3_dOase; 1.
DR   Pfam; PF03301; Trp_dioxygenase; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Dioxygenase; Heme; Iron; Metal-binding;
KW   Oxidoreductase; Tryptophan catabolism.
FT   CHAIN         1    403       Tryptophan 2,3-dioxygenase.
FT                                /FTId=PRO_0000072398.
FT   REGION       39     43       Substrate binding (By similarity).
FT   REGION       69     73       Substrate binding (By similarity).
FT   METAL       327    327       Iron (heme axial ligand) (By similarity).
FT   BINDING     140    140       Substrate (By similarity).
FT   BINDING     147    147       Heme (By similarity).
FT   BINDING     341    341       Substrate (By similarity).
SQ   SEQUENCE   403 AA;  46716 MW;  8F1E98075CA86A65 CRC64;
     MACPYLGSGE LTHRVTFMEG GEECQQGVNK VEMGFGQTYS EYLQLDKILT AQRLKSEADG
     QRVDDEHLFI VIHQAHELWF KQIIFDLDNV RKLLNNTIVD ETKTLKIVSG LDRMTKILSL
     LTEQITLLDT MSPLDFVDFR KYLTPASGFQ SLQFRVLENK LGVRQERRIK YNAQHYKNVF
     NDTDLKTLNV TEEEKSLLTL IESWLERTPG LKSTSEDEGF WIKYEKSVNK YLADLAKQAA
     DPSNTEEIAK QLTAEYHKTA DAFQSILDPR QHEQHIRNGN RLLSHDATKG AMMIYFYRDM
     PRFSQPYQIL TFLMDIDSLF TKWRYNHVLL VQRMLGAKQG TGGSSGYMYL RSTVSDRYKV
     FLDLFNLSTW LIPREYIPML SPRMVKTLSE HSNLSHSQSS ESD
//