allD

Ureidoglycolate dehydrogenase (NAD(+))

349 amino acids

AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin. It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions. Catalyzes the oxidation of ureidoglycolate to oxalurate.

Belongs to the LDH2/MDH2 oxidoreductase family.

37.891 kDa

MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILHADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLAFAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMIDVLSGVLLGLPFGRQVSSMYDDLHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRQAAVEGIEIVDDIYQYLISDALYNTSYETKNPFAQ

allD

Ureidoglycolate dehydrogenase (NAD(+))

349 amino acids

AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin (PubMed:10601204). It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions (PubMed:10601204). Catalyzes the oxidation of ureidoglycolate to oxalurate (PubMed:23284870).

Belongs to the LDH2/MDH2 oxidoreductase family.

37.967 kDa

MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILHADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGFIGISMCQSDPMVVPFGGAEIYYGTNPLAFAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGVPTTDPFAVHALLPAAGPKGYGLMMMIDVLSGVLLGLPFGRQVSSMYDDLHAGRNLGQLHIVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRKAAVEGIEIVDDIYQYLISDALYNTSYETKNPFAQ