B2FKN7 (T23O_STRMK) 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:	Smlt4336

Organism

Stenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]

Taxonomic identifier

522373 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Stenotrophomonas › Stenotrophomonas maltophilia group

Protein attributes

Sequence length	291 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 – 291	291	Tryptophan 2,3-dioxygenase		PRO_0000360138
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)
	B2FKN7 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: B5DFEB3A5A9DC13E	FASTA	291	33,574
	10 20 30 40 50 60 MSVDNNQRDL EAGIHTDLQG RLTYGGYLRL DQLLSAQQPL SSPPHHDEML FIIQHQTSEL 70 80 90 100 110 120 WLKLLGHELR AAIGFLQRDE VWQCRKVLAR SKQVLRQLTE QWSVLETLTP SEYMGFRDVL 130 140 150 160 170 180 GPSSGFQSLQ YRYIEFLLGN KNAQMLQVFE HDPAGQAQLR TVLEAPSLYE EFLKYLARFG 190 200 210 220 230 240 HAVPAVYEAH DWTQPHVADD ALQPVFERIY QDTDRYWREY ALCEDLVDLE TAFQLWRFRH 250 260 270 280 290 MRTVMRVIGF KRGTGGSSGV GFLAKALELT FFPELFQVRT SLQAAPPAEQ A

References

[1]

"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants." Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B. Genome Biol. 9:R74.1-R74.13(2008) [PubMed: 18419807] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K279a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM743169 Genomic DNA. Translation: CAQ47720.1.
RefSeq	YP_001974004.1. NC_010943.1.
3D structure databases
ProteinModelPortal	B2FKN7.
ModBase	Search...
Protein-protein interaction databases
STRING	B2FKN7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6394257.
GenomeReviews	Gene locus Smlt4336 in contig AM743169_GR.
KEGG	sml:Smlt4336.
PATRIC	23704117. VBISteMal45202_4105.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG647485.
OMA	QYREIEF.
ProtClustDB	CLSK539120.
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_STRMK

Accession

Primary (citable) accession number: B2FKN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	June 10, 2008
Last modified:	January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program