ID   T23O_BACMK              Reviewed;         279 AA.
AC   A9VHP7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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};
GN   OrderedLocusNames=BcerKBAB4_2557;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000903; ABY43761.1; -; Genomic_DNA.
DR   RefSeq; WP_002127699.1; NC_010184.1.
DR   AlphaFoldDB; A9VHP7; -.
DR   SMR; A9VHP7; -.
DR   STRING; 315730.BcerKBAB4_2557; -.
DR   EnsemblBacteria; ABY43761; ABY43761; BcerKBAB4_2557.
DR   KEGG; bwe:BcerKBAB4_2557; -.
DR   eggNOG; COG3483; Bacteria.
DR   HOGENOM; CLU_063240_0_0_9; -.
DR   OMA; WRWRNDH; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000002154; 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; IPR017485; Trp_2-3-dOase_bac.
DR   InterPro; IPR004981; Trp_2_3_dOase.
DR   PANTHER; PTHR10138; PTHR10138; 2.
DR   Pfam; PF03301; Trp_dioxygenase; 1.
DR   SUPFAM; SSF140959; SSF140959; 1.
DR   TIGRFAMs; TIGR03036; trp_2_3_diox; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase;
KW   Tryptophan catabolism.
FT   CHAIN           1..279
FT                   /note="Tryptophan 2,3-dioxygenase"
FT                   /id="PRO_0000360088"
FT   BINDING         48..52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         237
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         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
SQ   SEQUENCE   279 AA;  32733 MW;  B1614633979B67CA CRC64;
     MKENEKVIME KGIHTDFKEN MTYGEYLQLD SLLSSQQRLS DHHDEMLFIV IHQASELWMK
     LILHELNAAI ESIKQDKLPP AFKMLARVSK IQSQIIQSWD ILATLTPSEY IEFRDSLGQA
     SGFQSYQYRM IEYALGYKTP HALKIYEKDP ELHARLHKAL HTPSLYDVAI QALVKEGFPI
     HKDVLNRDIT QPYEEDATVE AAWIEVYADV QKYWDLYQLA EKLIDIEDWL QQWRFRHMKT
     VERIIGHKMG TGGSSGVSYL KRVLDQCFFP ELWNVRTKL