HMM Summary Page: TIGR03036
| Accession | TIGR03036 |
| Name | trp_2_3_diox |
| Function | tryptophan 2,3-dioxygenase |
| Gene Symbol | kynA |
| Trusted Cutoff | 390.70 |
| Domain Trusted Cutoff | 390.70 |
| Noise Cutoff | 118.90 |
| Domain Noise Cutoff | 118.90 |
| Isology Type | equivalog |
| EC Number | 1.13.11.11 |
| HMM Length | 264 |
| Mainrole Category | Energy metabolism |
| Subrole Category | Amino acids and amines |
| Gene Ontology Term | GO:0004833: tryptophan 2,3-dioxygenase activity molecular_function |
| GO:0019441: tryptophan catabolic process to kynurenine biological_process | |
| Author | Haft DH |
| Entry Date | Aug 7 2006 1:28PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | 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. |
| References | DR PFAM; PF03301; Tryptophan 2,3-dioxygenase RN [1] 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. RN [2] 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) |