Tryptophan 2,3-dioxygenase - Silicibacter pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)

Preferred order of sections

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:	SPOA0409

Encoded on

Plasmid megaplasmid Spo

Organism

Silicibacter pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) [Complete proteome] [HAMAP]

Taxonomic identifier

246200 [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	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)

Tools

Q5LKH2 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: F688B144068480AC
Show »

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

« Hide

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.

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. NC_006569.1.
3D structure databases
HSSP	HSSP built from PDB template 1YW0 based on UniProtKB Q8PDA8.
ProteinModelPortal	Q5LKH2.
SMR	Q5LKH2. Positions 18-278.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3196589.
GenomeReviews	Gene locus SPOA0409 in contig CP000032_GR.
KEGG	sil:SPOA0409.
NMPDR	fig\|246200.3.peg.405.
PATRIC	23382174. VBIRuePom114501_4410.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG647485.
OMA	QYREIEF.
ProtClustDB	CLSK751681.
Enzyme and pathway databases
BioCyc	RPOM246200:SPO_A0409-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_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 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents