ID   T23O_BOVIN              Reviewed;         406 AA.
AC   Q2KIQ5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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   Name=TDO2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Incorporates oxygen into the indole moiety of
CC       tryptophan. Has a broad specificity towards tryptamine and
CC       derivatives including D- and L-tryptophan, 5-hydroxytryptophan and
CC       serotonin (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   -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
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DR   EMBL; BC112550; AAI12551.1; -; mRNA.
DR   IPI; IPI00714687; -.
DR   RefSeq; NP_001039778.1; -.
DR   UniGene; Bt.55173; -.
DR   Ensembl; ENSBTAG00000011062; Bos taurus.
DR   GeneID; 530397; -.
DR   KEGG; bta:530397; -.
DR   HOVERGEN; Q2KIQ5; -.
DR   OMA; Q2KIQ5; HYRDNFR.
DR   BRENDA; 1.13.11.11; 251.
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: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   2: Evidence at transcript level;
KW   Coiled coil; Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase;
KW   Phosphoprotein; Tryptophan catabolism.
FT   CHAIN         1    406       Tryptophan 2,3-dioxygenase.
FT                                /FTId=PRO_0000247474.
FT   REGION       42     46       Substrate binding (By similarity).
FT   REGION       72     76       Substrate binding (By similarity).
FT   COILED      231    271       Potential.
FT   METAL       328    328       Iron (heme axial ligand) (By similarity).
FT   BINDING     144    144       Substrate (By similarity).
FT   BINDING     151    151       Heme (By similarity).
FT   BINDING     342    342       Substrate (By similarity).
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES     155    155       Phosphoserine (By similarity).
SQ   SEQUENCE   406 AA;  47708 MW;  D68CD8A6BC59A882 CRC64;
     MSGCPFLGKS FGYAFKPLSA QGSEEDKSQA GVNRASKGGL IYGNYLQLEK VLNAQELQSE
     MKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VITRMHRVVV
     ILKLLVQQFS VLETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQS LRVPYNRRHY
     RDNFRGKDNE LLLKSEQERT LLQLVEAWLE RTPGLEPHGF NFWGKLEKNI VKGLEEEFTK
     IQAKEESEEK EEQMAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYKALQ GALMIYFYRE
     EPRFQVPFQL LTFLMDVDSL MTKWRYNHVC LVHRMLGSKA GTGGSSGYQY LRSTVSDRYK
     VFVDLFNLST YLVPRHWIPK MNPVIHKFLY TAEYCDSSYF SSDESD
//