Q8PQ80 (T23O_XANAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan 2,3-dioxygenase
Short name=TDO
EC=1.13.11.11

Alternative name(s):
Tryptamin 2,3-dioxygenase
Tryptophan oxygenase
Short name=TO
Short name=TRPO
Tryptophan pyrrolase
Tryptophanase

Gene names

Name:	kynA
Ordered Locus Names:	XAC0448

Organism

Xanthomonas axonopodis pv. citri (Citrus canker) [Complete proteome] [HAMAP]

Taxonomic identifier

92829 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring By similarity.
Catalytic activity	L-tryptophan + O2 = N-formyl-L-kynurenine.
Cofactor	Binds 2 heme groups per tetramer By similarity.
Pathway	Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the tryptophan 2,3-dioxygenase family.

Ontologies

Keywords
Biological process	Tryptophan catabolism
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB tryptophan catabolic process to kynurenine Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	heme binding Inferred from sequence or structural similarity. Source: UniProtKB tryptophan 2,3-dioxygenase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 298	298	Tryptophan 2,3-dioxygenase		PRO_0000360139
Regions
	Region	24 – 28	5	Substrate binding By similarity
	Region	51 – 55	5	Substrate binding By similarity
Sites
	Metal binding	240	1	Iron (heme axial ligand) By similarity
	Binding site	113	1	Substrate By similarity
	Binding site	117	1	Substrate By similarity
	Binding site	124	1	Heme By similarity
	Binding site	254	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8PQ80 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 566F728331ADC97E	FASTA	298	34,470
	10 20 30 40 50 60 MPVDKNLRDL EPGIHTDLEG RLTYGGYLRL DQLLSAQQPL SEPAHHDEML FIIQHQTSEL 70 80 90 100 110 120 WLKLLAHELR AAIVHLQRDE VWQCRKVLAR SKQVLRQLTE QWSVLETLTP SEYMGFRDVL 130 140 150 160 170 180 GPSSGFQSLQ YRYIEFLLGN KNPQMLQVFA YDPQGQARLR EALEAPSLYE EFLRYLARFG 190 200 210 220 230 240 HAIPQQYQAR DWTAAHVADD SLRPVFERIY ENTDRYWREY ALCEDLVDVE TQFQLWRFRH 250 260 270 280 290 MRTVMRVIGF KRGTGGSSGV GFLQQALALT FFPELFDVRT SVGVETRSSQ GNAGTAGS

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." 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. Nature 417:459-463(2002) [PubMed: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 306.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008923 Genomic DNA. Translation: AAM35339.1.
RefSeq	NP_640803.1. NC_003919.1.
3D structure databases
HSSP	HSSP built from PDB template 1YW0 based on UniProtKB Q8PDA8.
ProteinModelPortal	Q8PQ80.
SMR	Q8PQ80. Positions 19-284.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1154519.
GenomeReviews	Gene locus XAC0448 in contig AE008923_GR.
KEGG	xac:XAC0448.
NMPDR	fig|190486.1.peg.447.
PATRIC	24052763. VBIXanAxo33670_0483.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG647485.
OMA	QYREIEF.
ProtClustDB	CLSK539120.
Enzyme and pathway databases
BioCyc	XAXO190486:XAC0448-MONOMER.
Family and domain databases
InterPro	IPR004981. Trp_2_3_dOase. [Graphical view]
KO	K00453.
PANTHER	PTHR10138. Trp_2_3_dOase. 1 hit.
Pfam	PF03301. Trp_dioxygenase. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

T23O_XANAC

Accession

Primary (citable) accession number: Q8PQ80

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program