|Function||4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit|
|Domain Trusted Cutoff||228.65|
|Domain Noise Cutoff||203.25|
|EC Number||126.96.36.199 188.8.131.52|
|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 . 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).|
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)|
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