| Accession | TIGR02305 |
| Name | HpaG-N-term |
| Function | 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit |
| Gene Symbol | hpaG |
| Trusted Cutoff | 228.65 |
| Domain Trusted Cutoff | 228.65 |
| Noise Cutoff | 203.25 |
| Domain Noise Cutoff | 203.25 |
| Isology Type | equivalog_domain |
| EC Number | 4.1.1.68 5.3.3.10 |
| HMM Length | 205 |
| Author | Selengut J |
| Entry Date | Sep 22 2004 11:32AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation [1]. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related C-terminal domain (TIGR02303). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED). |
| References | RN [1]
RM PMID: 11863436
RT The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold.
RA Tame JR, Namba K, Dodson EJ, Roper DI.
RL Biochemistry. 2002 Mar 5;41(9):2982-9. |
| Genome Property | GenProp0231: 4-hydroxyphenylacetate degradation (HMM) |
