|Domain Trusted Cutoff||223.05|
|Domain Noise Cutoff||179.75|
|Mainrole Category||Energy metabolism|
|Subrole Category||Amino acids and amines|
|Gene Ontology Term||GO:0004061: arylformamidase activity molecular_function|
| ||GO:0019441: tryptophan catabolic process to kynurenine biological_process|
|Entry Date||Aug 7 2006 12:07PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||One of several pathways of tryptophan degradation is as follows: tryptophan 2,3-dioxygenase (18.104.22.168) uses 02 to convert Trp to L-formylkynurenine. Arylformamidase (22.214.171.124) hydrolyzes the product to L-kynurenine and formate. Kynureninase (126.96.36.199) hydrolyzes L-kynurenine to anthranilate plus alanine. Members of the seed alignment for this model are bacterial predicted metal-dependent hydrolases. All are supported as arylformamidase (188.8.131.52) by an operon structure in which kynureninase and/or tryptophan 2,3-dioxygenase genes are adjacent. The members from Bacillus cereus, Pseudomonas aeruginosa and Ralstonia metallidurans were characterized. An example from Pseudomonas fluorescens is given the gene symbol qbsH instead of kynB because of its role in quinolobactin biosynthesis, which begins with tryptophan. All members of this family should be arylformamidase (184.108.40.206).|
RM PMID: 14592712
RT Aerobic tryptophan degradation pathway in bacteria: novel kynurenine formamidase.
RA Kurnasov O, Jablonski L, Polanuyer B, Dorrestein P, Begley T, Osterman A
RL FEMS Microbiol Lett. 2003 Oct 24;227(2):219-27.
RM PMID: 15066027
RT The Pseudomonas siderophore quinolobactin is synthesized from xanthurenic acid, an intermediate of the kynurenine pathway.
RA Matthijs S, Baysse C, Koedam N, Tehrani KA, Verheyden L, Budzikiewicz H, Schafer M, Hoorelbeke B, Meyer JM, De Greve H, Cornelis P
RL Mol Microbiol. 2004 Apr;52(2):371-84.|
|Genome Property||GenProp0659: tryptophan degradation to anthranilate (HMM)|
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