T23O2_RALSO
ID T23O2_RALSO Reviewed; 369 AA.
AC Q8XRY7;
DT 20-JAN-2009, 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 2 {ECO:0000255|HAMAP-Rule:MF_01972};
DE Short=TDO-2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01972};
DE AltName: Full=Tryptophan oxygenase 2 {ECO:0000255|HAMAP-Rule:MF_01972};
DE Short=TO-2 {ECO:0000255|HAMAP-Rule:MF_01972};
DE Short=TRPO-2 {ECO:0000255|HAMAP-Rule:MF_01972};
DE AltName: Full=Tryptophan pyrrolase 2 {ECO:0000255|HAMAP-Rule:MF_01972};
DE AltName: Full=Tryptophanase 2 {ECO:0000255|HAMAP-Rule:MF_01972};
GN Name=kynA2 {ECO:0000255|HAMAP-Rule:MF_01972}; OrderedLocusNames=RSp0694;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG Plasmid megaplasmid Rsp.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL646053; CAD17845.1; -; Genomic_DNA.
DR RefSeq; WP_011003992.1; NC_003296.1.
DR AlphaFoldDB; Q8XRY7; -.
DR SMR; Q8XRY7; -.
DR STRING; 267608.RSp0694; -.
DR EnsemblBacteria; CAD17845; CAD17845; RSp0694.
DR GeneID; 60503610; -.
DR KEGG; rso:RSp0694; -.
DR PATRIC; fig|267608.8.peg.4169; -.
DR eggNOG; COG3483; Bacteria.
DR HOGENOM; CLU_045599_1_1_4; -.
DR OMA; ERRHEHL; -.
DR UniPathway; UPA00333; UER00453.
DR Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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; 1.
DR Pfam; PF03301; Trp_dioxygenase; 1.
DR SUPFAM; SSF140959; SSF140959; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Plasmid;
KW Reference proteome; Tryptophan catabolism.
FT CHAIN 1..369
FT /note="Tryptophan 2,3-dioxygenase 2"
FT /id="PRO_0000360130"
FT BINDING 36..40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
FT BINDING 303
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 317
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972"
SQ SEQUENCE 369 AA; 42166 MW; 5554D0579E7E3161 CRC64;
MKPMSYWDYI KVEELLALQG GANGDETQVG NDEALFIVVH QVYELWFKLI LRELTFARDL
LRQDTVPGHQ IALGVRSLRR AIAVFEQANQ HFRVMETMTA RDFLDFRERL MPASGFQSAQ
LREIEILLGL EDNERIAVCQ GGSFKDALKL PNGALSSAAY RVEAREAHGQ SLKHCLYAWL
SRIPIDGSNE PAAVKRFLRD YIGSVRAESQ RRLQTAIDRQ LAPAEVERLR ARYQADDVGA
ETFLLAEEDP QADAMTREKR RAVRAAMLFV ESYRELPQLA WPRELLESIL ELEQSMLIWR
QRHARMVERI IGRRVGTGGS SGVDYLDQTA LRYRVFTDLW TVRSLLLRKS SVPPIRQGAS
YAFAEEALV
