Q0SFS2 (T23O_RHOSR) 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:	RHA1_ro01801

Organism

Rhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]

Taxonomic identifier

101510 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	284 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 – 284	284	Tryptophan 2,3-dioxygenase		PRO_0000360131
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)
	Q0SFS2 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 003EECBE23AED6AB	FASTA	284	32,390
	10 20 30 40 50 60 MGVQANTRAI EKDIVTDFSE RMSYASYLDL DTLLSAQKPV SRPEHHDELL FIIQHQTTEL 70 80 90 100 110 120 WLKLVLHETL AARAAFDEDD IGRALKCVAR VKHIQKTLTE QWSVLATLTP TEYSEFRRFL 130 140 150 160 170 180 GNSSGFQSYQ YRAVEFVLGN KNAGMLAVFE ADPAAHDLLG RLLAEPSLYD AFWQCLSRLG 190 200 210 220 230 240 YDVPASALDR DVTAAYTLNE DLLPLIKFVY ENHDEHWAVY EAFEEFVDLE ENFQLWRFRH 250 260 270 280 MRTVLRTIGM KSGTGGSSGV GFLQKALDLT FFPELLAVRT EIGR

References

[1]

"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse." McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D. Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed: 17030794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RHA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000431 Genomic DNA. Translation: ABG93614.1.
RefSeq	YP_701772.1. NC_008268.1.
3D structure databases
ProteinModelPortal	Q0SFS2.
SMR	Q0SFS2. Positions 23-284.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0SFS2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4218732.
GenomeReviews	Gene locus RHA1_ro01801 in contig CP000431_GR.
KEGG	rha:RHA1_ro01801.
PATRIC	23202429. VBIRhoJos26306_1820.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3483.
HOGENOM	HBG647485.
OMA	QYREIEF.
ProtClustDB	CLSK956673.
Enzyme and pathway databases
BioCyc	RSP101510:RHA1_RO01801-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_RHOSR

Accession

Primary (citable) accession number: Q0SFS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program