N-terminal domain of the monoamine oxidase C dehydratase
The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Feature 1:NADP binding site [chemical binding site]
Evidence:
Structure:2VRO; Aldehyde dehydrogenase from Burkholderia xenovorans Lb400 with NADPH bound in the cofactor-binding pocket, contacts determined at 3.5A - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",