T23O_PSEFL
ID T23O_PSEFL Reviewed; 284 AA.
AC Q84HF6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 48.
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};
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX PubMed=15066027; DOI=10.1111/j.1365-2958.2004.03999.x;
RA Matthijs S., Baysse C., Koedam N., Tehrani K.A., Verheyden L.,
RA Budzikiewicz H., Schaefer M., Hoorelbeke B., Meyer J.-M., De Greve H.,
RA Cornelis P.;
RT "The Pseudomonas siderophore quinolobactin is synthesized from xanthurenic
RT acid, an intermediate of the kynurenine pathway.";
RL Mol. Microbiol. 52:371-384(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 (By similarity). Required for synthesis of the
CC siderophore quinolobactin (PubMed:15066027). {ECO:0000255|HAMAP-
CC Rule:MF_01972, ECO:0000269|PubMed:15066027}.
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, ECO:0000269|PubMed:15066027}.
CC -!- PATHWAY: Siderophore biosynthesis; quinolobactin biosynthesis.
CC {ECO:0000269|PubMed:15066027}.
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; AY271621; AAL65288.1; -; Genomic_DNA.
DR RefSeq; WP_029293795.1; NZ_JENC01000007.1.
DR AlphaFoldDB; Q84HF6; -.
DR SMR; Q84HF6; -.
DR UniPathway; UPA00333; UER00453.
DR UniPathway; UPA00981; -.
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;
KW Tryptophan catabolism.
FT CHAIN 1..284
FT /note="Tryptophan 2,3-dioxygenase"
FT /id="PRO_0000360126"
FT BINDING 53..57
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 242
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 256
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
SQ SEQUENCE 284 AA; 33036 MW; B3B526C3454FCF42 CRC64;
MCPCPYMHQA KPQQWHDAKL DFAESMSYGD YLGLDKVLDA QVPRSQQHNE MLFIIQHQAS
ELWMKLLLHE LRHARQLIDQ GQLAGSHRVL ARVLRIMEQM VSSWAILATL SPMEFISFRS
DLGNASGFQS YQYREIEFIF GNKNRAMLLP HQHTPQIAKN LEQCLHTPSL YDAIIQQMTR
QDLPICALRL DADPSEPTRS DASVEAAWVQ VYRQPERYWD LYQLGEKLMD IEDAFRQWRF
RHVTVVERVI GFKKGTGGTE GVEYLRKMLG TVLFPELWSL RSSL
