Reviewed, UniProtKB/Swiss-Prot Q63AJ2 (T23O_BACCZ)

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:	BCE33L2486

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	279 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 – 279	279	Tryptophan 2,3-dioxygenase		PRO_0000360086
Regions
	Region	23 – 27	5	Substrate binding By similarity
	Region	48 – 52	5	Substrate binding By similarity
Sites
	Metal binding	237	1	Iron (heme axial ligand) By similarity
	Binding site	110	1	Substrate By similarity
	Binding site	114	1	Substrate By similarity
	Binding site	121	1	Heme By similarity
	Binding site	251	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63AJ2-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 6C26779E9B5BD0EA	FASTA	279	32,729
	10 20 30 40 50 60 MKENEKVIME KGIHTDFKEN MTYGEYLQLD SLLSSQKRLS DHHDEMLFIV IHQASELWMK 70 80 90 100 110 120 LILHELNAAI ESIKQDKLQP AFKMLARVSK IQSQIIQSWD ILATLTPSEY IEFRDSLGQA 130 140 150 160 170 180 SGFQSYQYRM IEYALGYKTP HALKIYEKDP ELHARLHAAL HAPSLYDVAI QALVKEGFPI 190 200 210 220 230 240 HKDVLNRDIT QPYEEDATVE AAWLEVYADV KKYWNLYQLA EKLIDIEDWL QQWRFRHMKT 250 260 270 VERIIGHKMG TGGSSGVSYL KRVLDQRFFP ELWNVRTKL

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000001 Genomic DNA. Translation: AAU17773.1.
RefSeq	YP_084075.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q63AJ2.
Genome annotation databases
GeneID	3023520.
GenomeReviews	Gene locus BCE33L2486 in contig CP000001_GR.
KEGG	bcz:BCZK2486.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q63AJ2.
OMA	MKLILHE.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L2486-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_BACCZ

Accession

Primary (citable) accession number: Q63AJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 29 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)