| Accession | TIGR02280 |
| Name | PaaB1 |
| Function | phenylacetate degradation probable enoyl-CoA hydratase PaaB |
| Gene Symbol | paaB |
| Trusted Cutoff | 345.15 |
| Domain Trusted Cutoff | 345.15 |
| Noise Cutoff | 303.40 |
| Domain Noise Cutoff | 303.40 |
| Isology Type | equivalog |
| EC Number | 4.2.1.17 |
| HMM Length | 256 |
| Gene Ontology Term | GO:0004300: enoyl-CoA hydratase activity molecular_function |
| | GO:0010124: phenylacetate catabolic process biological_process |
| Author | Selengut J |
| Entry Date | Aug 31 2004 2:49PM |
| Last Modified | Mar 1 2011 11:50AM |
| Comment | This family of proteins are found within apparent operons for the degradation of phenylacetic acid [1]. These proteins contain the enoyl-CoA hydratase domain as detected by PF00378. This activity is consistent with current hypotheses for the degradation pathway [2] which involve the ligation of phenylacetate with coenzyme A (paaF), hydroxylation (paaGHIJK), ring-opening (paaN) and degradation of the resulting fatty acid-like compound to a Krebs cycle intermediate (paaABCDE). |
| References | RN [1]
RM PMID: 11260461
RT The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications.
RA Luengo JM, Garcia JL, Olivera ER.
RL Mol Microbiol. 2001 Mar;39(6):1434-42.
RN [2]
RM PMID: 9748275
RT Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.
RA Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E.
RL J Biol Chem. 1998 Oct 2;273(40):25974-86. |
| Genome Property | GenProp0210: phenylacetic acid catabolism (HMM) |
