Reviewed, UniProtKB/Swiss-Prot Q5LKH2 (T23O_SILPO)

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:	SPOA0409

Encoded on

Plasmid megaplasmid Spo

Organism

Silicibacter pomeroyi [Complete proteome] [HAMAP]

Taxonomic identifier

89184 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Ruegeria

Protein attributes

Sequence length	278 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 Plasmid
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 – 278	278	Tryptophan 2,3-dioxygenase		PRO_0000360135
Regions
	Region	22 – 26	5	Substrate binding By similarity
	Region	47 – 51	5	Substrate binding By similarity
Sites
	Metal binding	236	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	250	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5LKH2-1 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: F688B144068480AC	FASTA	278	32,142
	10 20 30 40 50 60 MSQAYDPSQE GAKMSYAKDM SYGDYLHMDA LLATHHPQSD AHDEMLFIIQ HQTSELWMRL 70 80 90 100 110 120 VLHELRAARA LLLAGGDFRP AFKMLTRVAR IFDQLNSAWD VLRTMTPSDY TTFRNALGNS 130 140 150 160 170 180 SGFQSHQYRL IEYMLGNRNT AMMKVHEHRP ELHAMLAAEL EQPSLYHVAL RALAAKTGAS 190 200 210 220 230 240 FAPEVYRMDN PHSADAAVQA AWRQVYEDPA KYWDLYELGE KLVDLEDYFR RWRFNHVTTV 250 260 270 ERVIGFKRGT GGTSGVQYLR RMLEVELFPE LWHLRGDL

References

[1]

"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment." Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M. , Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N. Nature 432:910-913(2004) [PubMed: 15602564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700808 / DSM 15171 / DSS-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000032 Genomic DNA. Translation: AAV97540.1.
RefSeq	YP_165236.1.
3D structure databases
HSSP	HSSP built from PDB template 1YW0 based on UniProtKB Q8PDA8.
SMR	Q5LKH2. Positions 18-278.
ModBase	Search...
Genome annotation databases
GeneID	3196589.
GenomeReviews	Gene locus SPOA0409 in contig CP000032_GR.
KEGG	sil:SPOA0409.
NMPDR	fig|246200.3.peg.405.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG647485.
OMA	MKLILHE.
Enzyme and pathway databases
BioCyc	RPOM246200:SPO_A0409-MONOMER.
Family and domain databases
InterPro	IPR004981. Trp_2_3_dOase. [Graphical view]
PANTHER	PTHR10138. Trp_2_3_dOase. 1 hit.
Pfam	PF03301. Trp_dioxygenase. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

T23O_SILPO

Accession

Primary (citable) accession number: Q5LKH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	February 1, 2005
Last modified:	January 19, 2010
This is version 28 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)