T23O_BURCM
ID T23O_BURCM Reviewed; 308 AA.
AC Q0BCE0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 70.
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=Bamb_2627;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=ABI88183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000440; ABI88183.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041491259.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BCE0; -.
DR SMR; Q0BCE0; -.
DR STRING; 339670.Bamb_2627; -.
DR EnsemblBacteria; ABI88183; ABI88183; Bamb_2627.
DR GeneID; 44693290; -.
DR KEGG; bam:Bamb_2627; -.
DR PATRIC; fig|339670.21.peg.2274; -.
DR eggNOG; COG3483; Bacteria.
DR UniPathway; UPA00333; UER00453.
DR Proteomes; UP000000662; Chromosome 1.
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..308
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000360101"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77..81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 266
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 280
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
SQ SEQUENCE 308 AA; 35167 MW; E868A182F00E4B4A CRC64;
MQPPGDNAPA GCPFSGAHAA QPAHEAPHVP GDAAGEAGWH DAQLDFSKSM SYGDYLSLNS
ILDAQHPLSP DHNEMLFIIQ HQTSELWMKL ALFELRGALD AVRGDALPPA FKMLARVSRI
LEQLVQAWNV LSTMTPSEYS AMRPYLGQSS GFQSYQYRQL EFLLGNKNVQ MLQPHAHRPD
ILEQVRATLE APSFYDEVVR LLARRGFPIA PERLERDWTQ PMRHDETVEA AWLEVYRHPQ
QHWELYEMAE ELVDLEDAFR QWRFRHVTTV ERIIGFKQGT GGTSGAPYLR KMLDVVLFPE
LWHVRTTL
