Q6HHX9 (T23O_BACHK) 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:	BT9727_2521

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	279 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 – 279	279	Tryptophan 2,3-dioxygenase		PRO_0000360087
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)
	Q6HHX9 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: A61302B529A40203	FASTA	279	32,780
	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 HALKIYEKDQ ELHARLHTAL HAPSLYDVAI QALVKEGFSI 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]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT61838.1.
RefSeq	YP_036847.1. NC_005957.1.
3D structure databases
HSSP	HSSP built from PDB template 1YW0 based on UniProtKB Q8PDA8.
ProteinModelPortal	Q6HHX9.
SMR	Q6HHX9. Positions 20-279.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000074173; EBBACP00000072259; EBBACG00000074164.
GeneID	2857437.
GenomeReviews	Gene locus BT9727_2521 in contig AE017355_GR.
KEGG	btk:BT9727_2521.
NMPDR	fig|281309.1.peg.2487.
PATRIC	18985885. VBIBacThu119411_2669.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000004238.
HOGENOM	HBG647485.
OMA	KLLVDQV.
ProtClustDB	CLSK904616.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_2521-MONOMER.
Family and domain databases
InterPro	IPR017485. Trp_2-3-dOase_bac. IPR004981. Trp_2_3_dOase. [Graphical view]
KO	K00453.
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_BACHK

Accession

Primary (citable) accession number: Q6HHX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program