T23O1_RALSO
ID T23O1_RALSO Reviewed; 294 AA.
AC Q8Y1D2;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Tryptophan 2,3-dioxygenase 1 {ECO:0000255|HAMAP-Rule:MF_01972};
DE Short=TDO-1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01972};
DE AltName: Full=Tryptophan oxygenase 1 {ECO:0000255|HAMAP-Rule:MF_01972};
DE Short=TO-1 {ECO:0000255|HAMAP-Rule:MF_01972};
DE Short=TRPO-1 {ECO:0000255|HAMAP-Rule:MF_01972};
DE AltName: Full=Tryptophan pyrrolase 1 {ECO:0000255|HAMAP-Rule:MF_01972};
DE AltName: Full=Tryptophanase 1 {ECO:0000255|HAMAP-Rule:MF_01972};
GN Name=kynA1 {ECO:0000255|HAMAP-Rule:MF_01972}; OrderedLocusNames=RSc0758;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD14288.1; -; Genomic_DNA.
DR RefSeq; WP_011000712.1; NC_003295.1.
DR AlphaFoldDB; Q8Y1D2; -.
DR SMR; Q8Y1D2; -.
DR STRING; 267608.RSc0758; -.
DR EnsemblBacteria; CAD14288; CAD14288; RSc0758.
DR GeneID; 60500277; -.
DR KEGG; rso:RSc0758; -.
DR eggNOG; COG3483; Bacteria.
DR HOGENOM; CLU_063240_0_0_4; -.
DR OMA; WRWRNDH; -.
DR UniPathway; UPA00333; UER00453.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:UniProtKB-UniPathway.
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; 2.
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; Reference proteome;
KW Tryptophan catabolism.
FT CHAIN 1..294
FT /note="Tryptophan 2,3-dioxygenase 1"
FT /id="PRO_0000419537"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63..67
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 252
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 266
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
SQ SEQUENCE 294 AA; 34155 MW; 34289EC68ED8470B CRC64;
MSEPIQPTRP AASGCPMHGA QAESWHDAQM DFSKSMSYGD YLALDQILNA QHPRSPDHNE
MLFIVQHQTT ELWMKLMLHE LRAARDCVRN DDLPPAFKML ARVSRIMDQL VQAWNVLATM
TPPEYSAMRP HLGQSSGFQS YQYREIEFIL GNKNAAMLQP HAHQPEHYAQ VKAALETPSL
YDEAIRYMAR HGFAFDADCI ERDWSRPVTY NASVEAAWLE VYRDPTHHWE LYELAEKFVD
LEDAFRQWRF RHVTTVERVI GFKRGTGGTE GVNYLRKMLD VVLFPELWKL RTDL
