| Description | This entry represents a domain found in a group of succinate-semialdehyde dehydrogenases, including SSADH1 from Mycobacterium tuberculosis and Sad from Escherichia coli. Succinate-semialdehyde dehydrogenase 1 (SSADH1 or GabD1) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate [ ]. Sad catalyses the NAD+-dependent oxidation of succinate semialdehyde to succinate. It acts preferentially with NAD as cosubstrate but can also use NADP [, ].Proteins containing this domain also includes Aldh from Paenarthrobacter nicotinovorans. Aldh does not display succinate semialdehyde dehydrogenase activity. Instead, it acts as an aldehyde dehydrogenase involved in the oxidative D-xylose degradation pathway. It Is able to use both NAD+ and NADP+; however, it shows a preference for NADP+ [ ]. | Name | Succinate-semialdehyde dehydrogenase GabD1-like |
| Short Name | ALDH_GabD1-like | Type | Domain |
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