T23O_BACC1
ID T23O_BACC1 Reviewed; 279 AA.
AC Q736W5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=BCE_2785;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS41697.1; -; Genomic_DNA.
DR RefSeq; WP_000661937.1; NC_003909.8.
DR AlphaFoldDB; Q736W5; -.
DR SMR; Q736W5; -.
DR EnsemblBacteria; AAS41697; AAS41697; BCE_2785.
DR GeneID; 59159977; -.
DR KEGG; bca:BCE_2785; -.
DR HOGENOM; CLU_063240_0_0_9; -.
DR OMA; WRWRNDH; -.
DR UniPathway; UPA00333; UER00453.
DR Proteomes; UP000002527; 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_0000360085"
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; 32822 MW; 0882047AEC7F617F CRC64;
MKENEKIIME KGIHTDFKEN MTYGEYLQLD SLLSSQKRLS DHHDEMLFIV IHQASELWMK
LILHELYAAI ESIKQDKLQP AFKMLARVSK IQSQIIQSWD ILATLTPSEY IEFRDSLGQA
SGFQSYQYRM IEYALGYKTP HALKIYEKDP ELHARLHTAL HAPSLYDVAI QALVKEGFPI
HKDVLNRDIT QPYEEDATVE AAWLEVYADV KKYWNLYQLA EKLIDIEDWL QQWRFRHMKT
VERIIGHKMG TGGSSGVSYL KRVLDQRFFP ELWNVRTKL
