T23O_XANCP
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 03-AUG-2022, entry version 107.
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}; OrderedLocusNames=XCC0432;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; 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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01972,
CC 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; NP_635826.1; NC_003902.1.
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 PDBsum; 1YW0; -.
DR PDBsum; 2NW7; -.
DR PDBsum; 2NW8; -.
DR PDBsum; 2NW9; -.
DR PDBsum; 3BK9; -.
DR PDBsum; 3E08; -.
DR PDBsum; 7P46; -.
DR AlphaFoldDB; Q8PDA8; -.
DR SMR; Q8PDA8; -.
DR DIP; DIP-60795N; -.
DR STRING; 340.xcc-b100_0466; -.
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 OMA; WRWRNDH; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0019442; P:tryptophan catabolic process to acetyl-CoA; IBA:GO_Central.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IDA: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; 2.
DR Pfam; PF03301; Trp_dioxygenase; 2.
DR SUPFAM; SSF140959; SSF140959; 1.
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 L-
FT tryptophan, 5-fluoro-D/L-tryptophan, 6-fluoro-D/L-
FT tryptophan, 5-methyl-D/L-tryptophan and 6-methyl-D/L-
FT 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 L-
FT tryptophan, 5-fluoro-D/L-tryptophan, 6-fluoro-D/L-
FT tryptophan, 5-methyl-D/L-tryptophan and 6-methyl-D/L-
FT tryptophan as substrate."
FT /evidence="ECO:0000269|PubMed:17197414,
FT ECO:0000269|PubMed:18783250"
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 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 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
