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Tryptophan 2,3-dioxygenase (TDO) (EC 1.13.11.11) (Tryptamin 2,3-dioxygenase) (Tryptophan oxygenase) (TO) (TRPO) (Tryptophan pyrrolase) (Tryptophanase)

 T23O_XANCP              Reviewed;         298 AA.
Q8PDA8;
20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-OCT-2017, entry version 86.
RecName: Full=Tryptophan 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
Short=TDO {ECO:0000255|HAMAP-Rule:MF_01972};
EC=1.13.11.11 {ECO:0000255|HAMAP-Rule:MF_01972};
AltName: Full=Tryptamin 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
AltName: Full=Tryptophan oxygenase {ECO:0000255|HAMAP-Rule:MF_01972};
Short=TO {ECO:0000255|HAMAP-Rule:MF_01972};
Short=TRPO {ECO:0000255|HAMAP-Rule:MF_01972};
AltName: Full=Tryptophan pyrrolase {ECO:0000255|HAMAP-Rule:MF_01972};
AltName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_01972};
Name=kynA {ECO:0000255|HAMAP-Rule:MF_01972};
OrderedLocusNames=XCC0432;
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 /
NCPPB 528 / LMG 568 / P 25).
Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
Xanthomonadaceae; Xanthomonas.
NCBI_TaxID=190485;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
PubMed=12024217; DOI=10.1038/417459a;
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
Setubal J.C., Kitajima J.P.;
"Comparison of the genomes of two Xanthomonas pathogens with differing
host specificities.";
Nature 417:459-463(2002).
[2]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
L-TRYPTOPHAN AND HEME, FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, KINETIC PARAMETERS, HOMOTETRAMERIZATION, AND MUTAGENESIS
OF HIS-55.
PubMed=17197414; DOI=10.1073/pnas.0610007104;
Forouhar F., Anderson J.L.R., Mowat C.G., Vorobiev S.M., Hussain A.,
Abashidze M., Bruckmann C., Thackray S.J., Seetharaman J., Tucker T.,
Xiao R., Ma L.-C., Zhao L., Acton T.B., Montelione G.T., Chapman S.K.,
Tong L.;
"Molecular insights into substrate recognition and catalysis by
tryptophan 2,3-dioxygenase.";
Proc. Natl. Acad. Sci. U.S.A. 104:473-478(2007).
[3]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS ALA-55 AND SER-55 IN
COMPLEX WITH L-TRYPTOPHAN AND HEME, FUNCTION, CATALYTIC ACTIVITY,
KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
HOMOTETRAMERIZATION, AND MUTAGENESIS OF HIS-55.
PubMed=18783250; DOI=10.1021/bi801202a;
Thackray S.J., Bruckmann C., Anderson J.L.R., Campbell L.P., Xiao R.,
Zhao L., Mowat C.G., Forouhar F., Tong L., Chapman S.K.;
"Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base
but regulates catalysis by controlling substrate binding.";
Biochemistry 47:10677-10684(2008).
-!- FUNCTION: Heme-dependent dioxygenase that catalyzes the oxidative
cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-
tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative
cleavage of the indole moiety. {ECO:0000255|HAMAP-Rule:MF_01972,
ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250}.
-!- CATALYTIC ACTIVITY: L-tryptophan + O(2) = N-formyl-L-kynurenine.
{ECO:0000255|HAMAP-Rule:MF_01972, ECO:0000269|PubMed:17197414,
ECO:0000269|PubMed:18783250}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000255|HAMAP-Rule:MF_01972,
ECO:0000269|PubMed:18783250};
Note=Binds 1 heme group per subunit. {ECO:0000255|HAMAP-
Rule:MF_01972, ECO:0000269|PubMed:18783250};
-!- ENZYME REGULATION: Weakly inhibited by D-tryptophan.
{ECO:0000269|PubMed:17197414}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=114 uM for L-tryptophan {ECO:0000269|PubMed:17197414,
ECO:0000269|PubMed:18783250};
KM=100 uM for 5-fluoro-D/L-tryptophan
{ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250};
KM=186 uM for 6-fluoro-D/L-tryptophan
{ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250};
KM=357 uM for 5-methyl-D/L-tryptophan
{ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250};
KM=975 uM for 6-methyl-D/L-tryptophan
{ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250};
KM=119 uM for O(2) {ECO:0000269|PubMed:17197414,
ECO:0000269|PubMed:18783250};
-!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
{ECO:0000255|HAMAP-Rule:MF_01972}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01972,
ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250}.
-!- SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.
{ECO:0000255|HAMAP-Rule:MF_01972}.
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EMBL; AE008922; AAM39750.1; -; Genomic_DNA.
RefSeq; NP_635826.1; NC_003902.1.
RefSeq; WP_011035685.1; NC_003902.1.
PDB; 1YW0; X-ray; 2.70 A; A/B/C/D=23-298.
PDB; 2NW7; X-ray; 2.70 A; A/B/C/D=1-298.
PDB; 2NW8; X-ray; 1.60 A; A/B=1-298.
PDB; 2NW9; X-ray; 1.80 A; A/B=1-298.
PDB; 3BK9; X-ray; 2.15 A; A/B/C/D/E/F/G/H=1-298.
PDB; 3E08; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-298.
PDBsum; 1YW0; -.
PDBsum; 2NW7; -.
PDBsum; 2NW8; -.
PDBsum; 2NW9; -.
PDBsum; 3BK9; -.
PDBsum; 3E08; -.
ProteinModelPortal; Q8PDA8; -.
SMR; Q8PDA8; -.
DIP; DIP-60795N; -.
STRING; 190485.XCC0432; -.
EnsemblBacteria; AAM39750; AAM39750; XCC0432.
GeneID; 1000901; -.
KEGG; xcc:XCC0432; -.
PATRIC; fig|190485.4.peg.475; -.
eggNOG; ENOG4105HJ8; Bacteria.
eggNOG; COG3483; LUCA.
HOGENOM; HOG000221583; -.
KO; K00453; -.
OMA; YWDLYQL; -.
BRENDA; 1.13.11.11; 6708.
UniPathway; UPA00333; UER00453.
EvolutionaryTrace; Q8PDA8; -.
Proteomes; UP000001010; Chromosome.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004833; F:tryptophan 2,3-dioxygenase activity; IDA:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0019442; P:tryptophan catabolic process to acetyl-CoA; IBA:GO_Central.
GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IDA:UniProtKB.
HAMAP; MF_01972; T23O; 1.
InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
InterPro; IPR004981; Trp_2_3_dOase.
PANTHER; PTHR10138; PTHR10138; 2.
Pfam; PF03301; Trp_dioxygenase; 2.
SUPFAM; SSF140959; SSF140959; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Dioxygenase; Heme; Iron;
Metal-binding; Oxidoreductase; Reference proteome;
Tryptophan catabolism.
CHAIN 1 298 Tryptophan 2,3-dioxygenase.
/FTId=PRO_0000360143.
REGION 51 55 Substrate binding. {ECO:0000244|PDB:2NW8,
ECO:0000244|PDB:3BK9, ECO:0000255|HAMAP-
Rule:MF_01972,
ECO:0000269|PubMed:17197414,
ECO:0000269|PubMed:18783250}.
METAL 240 240 Iron (heme axial ligand).
{ECO:0000244|PDB:2NW7,
ECO:0000244|PDB:2NW8,
ECO:0000244|PDB:2NW9,
ECO:0000244|PDB:3BK9,
ECO:0000244|PDB:3E08, ECO:0000255|HAMAP-
Rule:MF_01972,
ECO:0000269|PubMed:17197414,
ECO:0000269|PubMed:18783250}.
BINDING 113 113 Substrate. {ECO:0000244|PDB:2NW8,
ECO:0000244|PDB:3BK9,
ECO:0000244|PDB:3E08, ECO:0000255|HAMAP-
Rule:MF_01972,
ECO:0000269|PubMed:17197414,
ECO:0000269|PubMed:18783250}.
BINDING 117 117 Substrate. {ECO:0000244|PDB:2NW8,
ECO:0000244|PDB:3BK9,
ECO:0000244|PDB:3E08, ECO:0000255|HAMAP-
Rule:MF_01972,
ECO:0000269|PubMed:17197414,
ECO:0000269|PubMed:18783250}.
BINDING 254 254 Substrate. {ECO:0000244|PDB:2NW8,
ECO:0000244|PDB:3BK9,
ECO:0000244|PDB:3E08, ECO:0000255|HAMAP-
Rule:MF_01972,
ECO:0000269|PubMed:17197414,
ECO:0000269|PubMed:18783250}.
MUTAGEN 55 55 H->A: Decrease in catalytic efficiency
using L-tryptophan, 5-fluoro-D/L-
tryptophan, 6-fluoro-D/L-tryptophan, 5-
methyl-D/L-tryptophan and 6-methyl-D/L-
tryptophan as substrate.
{ECO:0000269|PubMed:17197414,
ECO:0000269|PubMed:18783250}.
MUTAGEN 55 55 H->S: Decrease in catalytic efficiency
using L-tryptophan, 5-fluoro-D/L-
tryptophan, 6-fluoro-D/L-tryptophan, 5-
methyl-D/L-tryptophan and 6-methyl-D/L-
tryptophan as substrate.
{ECO:0000269|PubMed:17197414,
ECO:0000269|PubMed:18783250}.
HELIX 24 27 {ECO:0000244|PDB:2NW8}.
HELIX 30 33 {ECO:0000244|PDB:2NW8}.
HELIX 48 77 {ECO:0000244|PDB:2NW8}.
HELIX 81 100 {ECO:0000244|PDB:2NW8}.
HELIX 102 105 {ECO:0000244|PDB:2NW8}.
HELIX 110 113 {ECO:0000244|PDB:2NW8}.
TURN 114 116 {ECO:0000244|PDB:2NW8}.
HELIX 117 119 {ECO:0000244|PDB:2NW8}.
HELIX 125 127 {ECO:0000244|PDB:2NW8}.
HELIX 129 138 {ECO:0000244|PDB:2NW8}.
HELIX 143 146 {ECO:0000244|PDB:2NW8}.
TURN 148 151 {ECO:0000244|PDB:2NW8}.
HELIX 153 163 {ECO:0000244|PDB:2NW8}.
HELIX 168 178 {ECO:0000244|PDB:2NW8}.
HELIX 185 188 {ECO:0000244|PDB:2NW8}.
HELIX 200 202 {ECO:0000244|PDB:2NW8}.
HELIX 203 211 {ECO:0000244|PDB:2NW8}.
TURN 213 216 {ECO:0000244|PDB:2NW8}.
HELIX 217 248 {ECO:0000244|PDB:2NW8}.
STRAND 254 257 {ECO:0000244|PDB:2NW8}.
HELIX 260 266 {ECO:0000244|PDB:2NW8}.
HELIX 273 277 {ECO:0000244|PDB:2NW8}.
HELIX 278 280 {ECO:0000244|PDB:2NW8}.
TURN 281 283 {ECO:0000244|PDB:2NW8}.
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


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