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T23O_BURL3
ID   T23O_BURL3              Reviewed;         310 AA.
AC   Q39DG2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Bcep18194_A5910;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) 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}.
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DR   EMBL; CP000151; ABB09504.1; -; Genomic_DNA.
DR   RefSeq; WP_011353020.1; NC_007510.1.
DR   AlphaFoldDB; Q39DG2; -.
DR   SMR; Q39DG2; -.
DR   EnsemblBacteria; ABB09504; ABB09504; Bcep18194_A5910.
DR   GeneID; 45095793; -.
DR   KEGG; bur:Bcep18194_A5910; -.
DR   PATRIC; fig|482957.22.peg.2902; -.
DR   HOGENOM; CLU_063240_0_0_4; -.
DR   OMA; WRWRNDH; -.
DR   OrthoDB; 1660023at2; -.
DR   UniPathway; UPA00333; UER00453.
DR   Proteomes; UP000002705; 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..310
FT                   /note="Tryptophan 2,3-dioxygenase"
FT                   /id="PRO_0000360112"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         79..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT   BINDING         268
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         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
SQ   SEQUENCE   310 AA;  35300 MW;  02ECD0FC48D81BFB CRC64;
     MQPPGEDAPA GCPFSGARAA HSAPAAPAAH EASHVPGDAG WHNAQLDFSK SMSYGDYLSL
     NSILDAQHPL SPDHNEMLFI IQHQTSELWM KLALFELRGA LDAVRTDALP PAFKMLARVS
     RILEQLVQAW SVLSTMTPSE YSAMRPYLGQ SSGFQSYQYR QLEFLLGNKN VQMLQPHAHR
     PDILEQVRAT LEAPSFYDEV VRLLARRGFP IAAERLERDW TQPTRHDETV EAAWLEVYRH
     PQQHWELYEM AEELVDLEDA FRQWRFRHVT TVERIIGFKQ GTGGTSGAPY LRKMLDVVLF
     PELWHVRTTL
 
 
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