ID Q0APM6_MARMM Unreviewed; 282 AA. AC Q0APM6; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 02-SEP-2026, entry version 99. 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=Mmar10_1469 {ECO:0000313|EMBL:ABI65761.1}; OS Maricaulis maris (strain MCS10) (Caulobacter maris). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Maricaulales; Maricaulaceae; Maricaulis. OX NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI65761.1, ECO:0000313|Proteomes:UP000001964}; RN [1] {ECO:0000313|EMBL:ABI65761.1, ECO:0000313|Proteomes:UP000001964} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS10 {ECO:0000313|EMBL:ABI65761.1, RC ECO:0000313|Proteomes:UP000001964}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., RA Stephens C., Richardson P.; RT "Complete sequence of Maricaulis maris MCS10."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000449; ABI65761.1; -; Genomic_DNA. DR RefSeq; WP_011643408.1; NC_008347.1. DR AlphaFoldDB; Q0APM6; -. DR STRING; 394221.Mmar10_1469; -. DR KEGG; mmr:Mmar10_1469; -. DR eggNOG; COG3483; Bacteria. DR HOGENOM; CLU_063240_0_0_5; -. DR OrthoDB; 9776847at2; -. DR UniPathway; UPA00333; UER00453. DR Proteomes; UP000001964; Chromosome. 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 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 NCBIfam; TIGR03036; trp_2_3_diox; 1. 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. 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:UP000001964}; KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP- KW Rule:MF_01972}. FT BINDING 51..55 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01972" FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01972" FT BINDING 117 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01972" 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:0000256|HAMAP-Rule:MF_01972" FT BINDING 254 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01972" SQ SEQUENCE 282 AA; 32613 MW; 213843DBAFA9C6A4 CRC64; MSETFSSRVD VSGEDIHWDF KDEMSYGGYL SLDVLLAAQT PLTDEHDEML FVVIHHVAEL WMKLLLHETG AALEDLRQDN AGPALKKFAR VSRIQEQLTQ AWEVLATMTP TDYLAFRDKL GASSGFQSFQ YRTLEYRLGN KNAALARVHA SNPPAFKMVN DALQRPSLWD ETLRWLSRKG YDIPADRLER DWSQSYEASA AVEDVWRTIY RDSETHWEAY ELGEKLVDLE HKFQQWRFNH MKTVERIIGF RRGTGGTGGV SYLVKALDLR FFPEIWTVRT SL //