ID B2JDS2_PARP8 Unreviewed; 311 AA. AC B2JDS2; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 04-NOV-2026, entry version 87. DE RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000256|HAMAP-Rule:MF_01972}; DE Short=TDO {ECO:0000256|HAMAP-Rule:MF_01972}; DE EC=1.13.11.11 {ECO:0000256|HAMAP-Rule:MF_01972}; DE AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000256|HAMAP-Rule:MF_01972}; DE AltName: Full=Tryptophan oxygenase {ECO:0000256|HAMAP-Rule:MF_01972}; DE Short=TO {ECO:0000256|HAMAP-Rule:MF_01972}; DE Short=TRPO {ECO:0000256|HAMAP-Rule:MF_01972}; DE AltName: Full=Tryptophan pyrrolase {ECO:0000256|HAMAP-Rule:MF_01972}; DE AltName: Full=Tryptophanase {ECO:0000256|HAMAP-Rule:MF_01972}; GN Name=kynA {ECO:0000256|HAMAP-Rule:MF_01972}; GN OrderedLocusNames=Bphy_0506 {ECO:0000313|EMBL:ACC69698.1}; OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / OS STM815) (Burkholderia phymatum). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC69698.1, ECO:0000313|Proteomes:UP000001192}; RN [1] {ECO:0000313|Proteomes:UP000001192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815 RC {ECO:0000313|Proteomes:UP000001192}; RX PubMed=25197461; DOI=10.4056/sigs.4861021; RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R., RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D., RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M., RA Bristow J., Riley M.; RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host RT range and efficient nitrogen-fixing symbiont of Mimosa species."; RL Stand. Genomic Sci. 9:763-774(2014). 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00050412, ECO:0000256|HAMAP- CC Rule:MF_01972}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01972}; CC Note=Binds 1 heme group per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01972}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881, CC ECO:0000256|HAMAP-Rule:MF_01972}. CC -!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family. CC {ECO:0000256|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; CP001043; ACC69698.1; -; Genomic_DNA. DR RefSeq; WP_012399923.1; NC_010622.1. DR STRING; 391038.Bphy_0506; -. DR KEGG; bph:Bphy_0506; -. DR eggNOG; COG3483; Bacteria. DR HOGENOM; CLU_063240_0_0_4; -. DR OMA; AADRGQY; -. DR OrthoDB; 9776847at2; -. DR UniPathway; UPA00333; UER00453. 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; IPR017485; Trp_2-3-dOase_bac. 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; 1. DR SUPFAM; SSF140959; Indolic compounds 2,3-dioxygenase-like; 1. DR NCBIfam; TIGR03036; trp_2_3_diox; 1. DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule. DR GO; GO:0004833; F:L-tryptophan 2,3-dioxygenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0006569; P:L-tryptophan catabolic process; IEA:InterPro. DR Proteomes; UP000001192; Chromosome 1. DR AlphaFoldDB; B2JDS2; -. PE 3: Inferred from homology; KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|HAMAP- KW Rule:MF_01972}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01972}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01972}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01972}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01972}; Reference proteome {ECO:0000313|Proteomes:UP000001192}; KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP- KW Rule:MF_01972}. FT BINDING 80..84 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01972" FT BINDING 142 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01972" FT BINDING 146 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01972" FT BINDING 269 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:0000256|HAMAP-Rule:MF_01972" FT BINDING 283 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01972" SQ SEQUENCE 311 AA; 35753 MW; 88E110049CAA09B7 CRC64; MTDHMKMMEA TPAQGCPFGH GGTPTLRTDH ASHMAVDEGE GWHDAQLDFS KSMSYGDYLS LGSILRAQHP LSPDHNEMLF IIQHQTSELW MKLALYELRA ALACVHRDEL PPAFKMLARV SRILEQLVQA WNVLSTMTPS EYTSMRPFLG SSSGFQSYQY RELEFMLGNK NEQMLKPHAH HPDVLAEVKA ALEAPSFYDE VIRLLSRRGF AIDSSRLERD WTQPTVYDAS VEAAWLEVYR NPSQHWELYE MAEELVDLED AFRQWRFRHV TTVERIIGFK QGTGGTSGAP YLRKMLDVVL FPELWQVRTM L //