ID   T23O_MYXXD              Reviewed;         291 AA.
AC   Q1CVR6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
DE            Short=TDO {ECO:0000255|HAMAP-Rule:MF_01972};
DE            EC=1.13.11.11 {ECO:0000255|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophan oxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
DE            Short=TO {ECO:0000255|HAMAP-Rule:MF_01972};
DE            Short=TRPO {ECO:0000255|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophan pyrrolase {ECO:0000255|HAMAP-Rule:MF_01972};
DE   AltName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_01972};
GN   Name=kynA {ECO:0000255|HAMAP-Rule:MF_01972}; OrderedLocusNames=MXAN_7400;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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_01972}.
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_01972};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01972};
CC       Note=Binds 1 heme group per subunit. {ECO:0000255|HAMAP-Rule:MF_01972};
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_01972}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01972}.
CC   -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01972}.
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DR   EMBL; CP000113; ABF86173.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1CVR6; -.
DR   SMR; Q1CVR6; -.
DR   STRING; 246197.MXAN_7400; -.
DR   EnsemblBacteria; ABF86173; ABF86173; MXAN_7400.
DR   KEGG; mxa:MXAN_7400; -.
DR   eggNOG; COG3483; Bacteria.
DR   HOGENOM; CLU_063240_0_0_7; -.
DR   OMA; WRWRNDH; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000002402; Chromosome.
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: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; 2.
DR   Pfam; PF03301; Trp_dioxygenase; 2.
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..291
FT                   /note="Tryptophan 2,3-dioxygenase"
FT                   /id="PRO_0000360119"
FT   BINDING         51..55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         240
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_01972"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
SQ   SEQUENCE   291 AA;  34295 MW;  A5ECE46C4AE3054A CRC64;
     MPGPMNKRDL EPGIITDLAG RTTYGDYLQL DRLLSAQVTR SQPPHHDELL FIIQHQTSEL
     WMKLLIHELG ACIRYVQADR LEPSFKIFAR VAHIQRMLFE QWSVLETLTP NEYLEFRDTL
     GSSSGFQSFQ YRAVEFLLGN KDAQALMPFR HVPAIHGELE RLFESPSLYD EFLRHLSRMG
     HPVPQSHVQR DWRKPYEKSP EVVEVFRRIY QDAEAHWDAY EMCEKLVDTE ERFQLWRYRH
     MMTVMRIIGF KQGTGGSSGV GFLRKALDLR FFPELWDVRT ELTPPPPRHR P