Reviewed, UniProtKB/Swiss-Prot Q63WP5 (T23O_BURPS)

Names and origin

Protein names

Recommended name:
    Tryptophan 2,3-dioxygenase
      Short name=TDO
    EC=1.13.11.11
Alternative name(s):
    Tryptophan pyrrolase
      Short name=Tryptophanase
    Tryptophan oxygenase
      Short name=TRPO
      Short name=TO
    Tryptamin 2,3-dioxygenase

Gene names

Name:	kynA
Ordered Locus Names:	BPSL0846

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP]

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	306 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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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 – 306	306	Tryptophan 2,3-dioxygenase		PRO_0000360111
Regions
	Region	50 – 54	5	Substrate binding By similarity
	Region	75 – 79	5	Substrate binding By similarity
Sites
	Metal binding	264	1	Iron (heme axial ligand) By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	148	1	Heme By similarity
	Binding site	278	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63WP5-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 2C27E8FCE42E6F7C	FASTA	306	34,813
	10 20 30 40 50 60 MQPPGDDAAP RCPFAGAHAP DAPHVPEAAG DDAQAGWHRA QLDFSQSMSY GDYLSLDPIL 70 80 90 100 110 120 DAQHPRSPDH NEMLFIIQHQ TSELWMKLAL YELRAALASI RDDALPPAFK MLARVSRVLE 130 140 150 160 170 180 QLVQAWNVLA TMTPSEYSAM RPYLGASSGF QSYQYRELEF ILGNKNAQML RPHAHRPAIH 190 200 210 220 230 240 AHLEASLQAP SLYDEVIRLL ARRGFPIAPE RLDADWTQPT RHDRTVEAAW LAVYREPNAH 250 260 270 280 290 300 WELYEMAEEL VDLEDAFRQW RFRHVTTVER IIGFKQGTGG TSGAPYLRKM LDVVLFPELW HVRTTL

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571965 Genomic DNA. Translation: CAH34838.1.
RefSeq	YP_107471.1.
3D structure databases
HSSP	HSSP built from PDB template 1YW0 based on UniProtKB Q8PDA8.
SMR	Q63WP5. Positions 46-306.
ModBase	Search...
Genome annotation databases
GeneID	3092668.
GenomeReviews	Gene locus BPSL0846 in contig BX571965_GR.
KEGG	bps:BPSL0846.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG647485.
OMA	MKLILHE.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL0846-MONOMER.
Family and domain databases
InterPro	IPR017485. Trp_2-3-dOase_bac. IPR004981. Trp_2_3_dOase. [Graphical view]
PANTHER	PTHR10138. Trp_2_3_dOase. 1 hit.
Pfam	PF03301. Trp_dioxygenase. 1 hit. [Graphical view]
TIGRFAMs	TIGR03036. trp_2_3_diox. 1 hit.
ProtoNet	Search...

Entry information

Entry name

T23O_BURPS

Accession

Primary (citable) accession number: Q63WP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	October 25, 2004
Last modified:	February 9, 2010
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)