ID T23O_XANCP Reviewed; 298 AA. AC Q8PDA8; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 02-SEP-2026, entry version 118. 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=XCC0432; OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB OS 528 / LMG 568 / P 25). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Lysobacterales; Lysobacteraceae; Xanthomonas. OX NCBI_TaxID=190485; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(2002). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH RP L-TRYPTOPHAN AND HEME, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, RP KINETIC PARAMETERS, HOMOTETRAMERIZATION, AND MUTAGENESIS OF HIS-55. RX PubMed=17197414; DOI=10.1073/pnas.0610007104; RA Forouhar F., Anderson J.L.R., Mowat C.G., Vorobiev S.M., Hussain A., RA Abashidze M., Bruckmann C., Thackray S.J., Seetharaman J., Tucker T., RA Xiao R., Ma L.-C., Zhao L., Acton T.B., Montelione G.T., Chapman S.K., RA Tong L.; RT "Molecular insights into substrate recognition and catalysis by tryptophan RT 2,3-dioxygenase."; RL Proc. Natl. Acad. Sci. U.S.A. 104:473-478(2007). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS ALA-55 AND SER-55 IN RP COMPLEX WITH L-TRYPTOPHAN AND HEME, FUNCTION, CATALYTIC ACTIVITY, KINETIC RP PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, HOMOTETRAMERIZATION, RP AND MUTAGENESIS OF HIS-55. RX PubMed=18783250; DOI=10.1021/bi801202a; RA Thackray S.J., Bruckmann C., Anderson J.L.R., Campbell L.P., Xiao R., RA Zhao L., Mowat C.G., Forouhar F., Tong L., Chapman S.K.; RT "Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but RT regulates catalysis by controlling substrate binding."; RL Biochemistry 47:10677-10684(2008). 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 ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250}. 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, ECO:0000269|PubMed:17197414, CC ECO:0000269|PubMed:18783250}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01972, ECO:0000269|PubMed:18783250}; CC Note=Binds 1 heme group per subunit. {ECO:0000255|HAMAP-Rule:MF_01972, CC ECO:0000269|PubMed:18783250}; CC -!- ACTIVITY REGULATION: Weakly inhibited by D-tryptophan. CC {ECO:0000269|PubMed:17197414}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=114 uM for L-tryptophan {ECO:0000269|PubMed:17197414, CC ECO:0000269|PubMed:18783250}; CC KM=100 uM for 5-fluoro-D/L-tryptophan {ECO:0000269|PubMed:17197414, CC ECO:0000269|PubMed:18783250}; CC KM=186 uM for 6-fluoro-D/L-tryptophan {ECO:0000269|PubMed:17197414, CC ECO:0000269|PubMed:18783250}; CC KM=357 uM for 5-methyl-D/L-tryptophan {ECO:0000269|PubMed:17197414, CC ECO:0000269|PubMed:18783250}; CC KM=975 uM for 6-methyl-D/L-tryptophan {ECO:0000269|PubMed:17197414, CC ECO:0000269|PubMed:18783250}; CC KM=119 uM for O(2) {ECO:0000269|PubMed:17197414, CC ECO:0000269|PubMed:18783250}; 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 ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250}. 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; AE008922; AAM39750.1; -; Genomic_DNA. DR RefSeq; WP_011035685.1; NC_003902.1. DR PDB; 1YW0; X-ray; 2.70 A; A/B/C/D=23-298. DR PDB; 2NW7; X-ray; 2.70 A; A/B/C/D=1-298. DR PDB; 2NW8; X-ray; 1.60 A; A/B=1-298. DR PDB; 2NW9; X-ray; 1.80 A; A/B=1-298. DR PDB; 3BK9; X-ray; 2.15 A; A/B/C/D/E/F/G/H=1-298. DR PDB; 3E08; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-298. DR PDB; 7P46; X-ray; 1.70 A; A/B/C/D/E/F/G/H=5-286. DR AlphaFoldDB; Q8PDA8; -. DR SMR; Q8PDA8; -. DR DIP; DIP-60795N; -. DR STRING; 190485.XCC0432; -. DR EnsemblBacteria; AAM39750; AAM39750; XCC0432. DR GeneID; 58011747; -. DR KEGG; xcc:XCC0432; -. DR PATRIC; fig|190485.4.peg.475; -. DR eggNOG; COG3483; Bacteria. DR HOGENOM; CLU_063240_0_0_6; -. DR OrthoDB; 9776847at2; -. DR BRENDA; 1.13.11.11; 9230. DR BRENDA; 1.13.11.52; 6708. DR SABIO-RK; Q8PDA8; -. DR UniPathway; UPA00333; UER00453. DR EvolutionaryTrace; Q8PDA8; -. DR Proteomes; UP000001010; Chromosome. DR GO; GO:0020037; F:heme binding; IDA:UniProtKB. DR GO; GO:0004833; F:L-tryptophan 2,3-dioxygenase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR FunFam; 1.20.58.480:FF:000001; Tryptophan 2,3-dioxygenase; 1. DR Gene3D; 1.20.58.480; -; 1. 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; TRYPTOPHAN 2,3-DIOXYGENASE; 1. DR PANTHER; PTHR10138:SF0; TRYPTOPHAN 2,3-DIOXYGENASE; 1. DR Pfam; PF03301; Trp_dioxygenase; 2. DR SUPFAM; SSF140959; Indolic compounds 2,3-dioxygenase-like; 1. DR PDBsum; 1YW0; -. DR PDBsum; 2NW7; -. DR PDBsum; 2NW8; -. DR PDBsum; 2NW9; -. DR PDBsum; 3BK9; -. DR PDBsum; 3E08; -. DR PDBsum; 7P46; -. PE 1: Evidence at protein level; KW 3D-structure; Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; KW Reference proteome; Tryptophan catabolism. FT CHAIN 1..298 FT /note="Tryptophan 2,3-dioxygenase" FT /id="PRO_0000360143" FT BINDING 51..55 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972, FT ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, FT ECO:0007744|PDB:2NW8, ECO:0007744|PDB:3BK9" FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972, FT ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, FT ECO:0007744|PDB:2NW8, ECO:0007744|PDB:3BK9, FT ECO:0007744|PDB:3E08" FT BINDING 117 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972, FT ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, FT ECO:0007744|PDB:2NW8, ECO:0007744|PDB:3BK9, FT ECO:0007744|PDB:3E08" FT BINDING 240 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 ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, FT ECO:0007744|PDB:2NW7, ECO:0007744|PDB:2NW8, FT ECO:0007744|PDB:2NW9, ECO:0007744|PDB:3BK9, FT ECO:0007744|PDB:3E08" FT BINDING 254 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01972, FT ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, FT ECO:0007744|PDB:2NW8, ECO:0007744|PDB:3BK9, FT ECO:0007744|PDB:3E08" FT MUTAGEN 55 FT /note="H->A: Decrease in catalytic efficiency using FT L-tryptophan, 5-fluoro-D/L-tryptophan, FT 6-fluoro-D/L-tryptophan, 5-methyl-D/L-tryptophan and FT 6-methyl-D/L-tryptophan as substrate." FT /evidence="ECO:0000269|PubMed:17197414, FT ECO:0000269|PubMed:18783250" FT MUTAGEN 55 FT /note="H->S: Decrease in catalytic efficiency using FT L-tryptophan, 5-fluoro-D/L-tryptophan, FT 6-fluoro-D/L-tryptophan, 5-methyl-D/L-tryptophan and FT 6-methyl-D/L-tryptophan as substrate." FT /evidence="ECO:0000269|PubMed:17197414, FT ECO:0000269|PubMed:18783250" FT HELIX 8..11 FT /evidence="ECO:0007829|PDB:7P46" FT HELIX 24..27 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 30..33 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 48..77 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 81..100 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 102..105 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 110..113 FT /evidence="ECO:0007829|PDB:2NW8" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 129..138 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 143..146 FT /evidence="ECO:0007829|PDB:2NW8" FT TURN 148..151 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 153..163 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 168..178 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 185..188 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 195..198 FT /evidence="ECO:0007829|PDB:3E08" FT HELIX 200..202 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 203..211 FT /evidence="ECO:0007829|PDB:2NW8" FT TURN 213..216 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 217..248 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:2NW8" FT STRAND 254..257 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 260..266 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 273..277 FT /evidence="ECO:0007829|PDB:2NW8" FT HELIX 278..280 FT /evidence="ECO:0007829|PDB:2NW8" FT TURN 281..283 FT /evidence="ECO:0007829|PDB:2NW8" SQ SEQUENCE 298 AA; 34617 MW; 544600380EDD4A3D CRC64; MPVDKNLRDL EPGIHTDLEG RLTYGGYLRL DQLLSAQQPL SEPAHHDEML FIIQHQTSEL WLKLLAHELR AAIVHLQRDE VWQCRKVLAR SKQVLRQLTE QWSVLETLTP SEYMGFRDVL GPSSGFQSLQ YRYIEFLLGN KNPQMLQVFA YDPAGQARLR EVLEAPSLYE EFLRYLARFG HAIPQQYQAR DWTAAHVADD TLRPVFERIY ENTDRYWREY SLCEDLVDVE TQFQLWRFRH MRTVMRVIGF KRGTGGSSGV GFLQQALALT FFPELFDVRT SVGVDNRPPQ GSADAGKR //