Reviewed, UniProtKB/Swiss-Prot Q7WHE8 (T23O_BORBR)

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:	BB3260

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 – 284	284	Tryptophan 2,3-dioxygenase		PRO_0000360090
Regions
	Region	28 – 32	5	Substrate binding By similarity
	Region	53 – 57	5	Substrate binding By similarity
Sites
	Metal binding	242	1	Iron (heme axial ligand) By similarity
	Binding site	115	1	Substrate By similarity
	Binding site	119	1	Substrate By similarity
	Binding site	126	1	Heme By similarity
	Binding site	256	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WHE8-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 8E130F8D7C5533FF	FASTA	284	32,942
	10 20 30 40 50 60 MQPTPTQRPE AIVHDEKAQL DFARDMSYGD YLHLDELLGA QHPLSPEHNE MLFIVQHQTS 70 80 90 100 110 120 ELWMKLMLHE LRAAIAAIQQ DRLQPAFKML ARVSKILEQL VSAWDVLATM TPPEYSALRP 130 140 150 160 170 180 YLAHSSGFQS YQYRQIEYLL GNKNAAMLQP HAHRADLLAQ VRAAFEAPSL YDEALRFLAR 190 200 210 220 230 240 SGLAVPAGAL QRDWTQPYRA DDQVEQAWLT VYRQSERYWN QYQLGEKLTD LEDAFRLWRF 250 260 270 280 RHVTTVERII GFKRGTGGTS GVTYLRKMLE VVLFPEIWKL RTDL

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640447 Genomic DNA. Translation: CAE33752.1.
RefSeq	NP_889796.1.
3D structure databases
SMR	Q7WHE8. Positions 24-284.
ModBase	Search...
Genome annotation databases
GeneID	2661433.
GenomeReviews	Gene locus BB3260 in contig BX470250_GR.
KEGG	bbr:BB3260.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7WHE8.
OMA	QWSVLAT.
Enzyme and pathway databases
BioCyc	BBRO257310:BB3260-MON.
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_BORBR

Accession

Primary (citable) accession number: Q7WHE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 30 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)