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InterPro: IPR017485 Tryptophan 2,3-dioxygenase, bacteria

Protein matchesHelp
UniProtKB
Matches:
197 proteins
AccessionHelp IPR017485 Trp_2-3-dOase_bac
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR004981 Tryptophan 2,3-dioxygenase
GO Term annotationHelp
Process GO:0055114 oxidation reduction
Function GO:0004833 tryptophan 2,3-dioxygenase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Members of this family are tryptophan 2,3-dioxygenase, as confirmed by several experimental characterizations, and by conserved operon structure for many of the other members. This enzyme represents the first of a two-step degradation to L-kynurenine, and a three-step pathway (via kynurenine) to anthranilate plus alanine.

Database linksHelp
Enzyme: EC:1.13.11.11

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR017485 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
Q1LK00 Tryptophan 2,3-dioxygenase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017485 Tryptophan 2,3-dioxygenase, bacteria
IPR004981 Tryptophan 2,3-dioxygenase
PDB Chain

PublicationsHelp

Additional ReadingHelp
Matthijs S, Baysse C, Koedam N, Tehrani KA, Verheyden L, Budzikiewicz H, Schafer M, Hoorelbeke B, Meyer JM, De Greve H, Cornelis P.
The Pseudomonas siderophore quinolobactin is synthesized from xanthurenic acid, an intermediate of the kynurenine pathway.
Mol. Microbiol. 52 2004 371-84 [PubMed: 15066027]
http://dx.doi.org/10.1111/j.1365-2958.2004.03999.x
Kurnasov O, Jablonski L, Polanuyer B, Dorrestein P, Begley T, Osterman A.
Aerobic tryptophan degradation pathway in bacteria: novel kynurenine formamidase.
FEMS Microbiol. Lett. 227 2003 219-27 [PubMed: 14592712]
http://dx.doi.org/10.1016/S0378-1097(03)00684-0
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InterPro 23.1