CsiD

• PFAM accession number: PF08943
• Interpro abstract (IPR015038):

  GlaH (also known as CsiD) acts as an alpha-ketoglutarate-dependent dioxygenase catalyzing hydroxylation of glutarate (GA) to L-2-hydroxyglutarate (L2HG) in the stationary phase of E.coli. It functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. Other dicarboxylic acids (oxalate, malonate, succinate, adipate, and pimelate) are not substrates for this enzyme [ (PUBMED:30498244) ].

• GO function: oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, with 2-oxoglutarate as one donor, and the other dehydrogenated (GO:0050498), iron ion binding (GO:0005506)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry CsiD