| Primary Identifier | IPR016426 | Type | Family |
| Short Name | MA1821-like |
| description | In Methanosarcina acetivorans, MA1821 is a L-aspartate semialdehyde sulfurtransferase required for O-acetylhomoserine sulfhydrylase (OAHS)-independent homocysteine (Hcy) biosynthesis [, ]. It contains two C-terminal cystathionine beta-synthase (CBS) domains. The CBS domains bind S-adenosyl-l-methionine (SAM) and 5'-methylthioadenosine (MTA), which induce a conformational change consistent with regulatory function. Another protein in the same pathway, MA1822, is involved in the reduction of the disulfide formed in MA1821 during the conversion of Asa (aspartate semialdehyde) to Hcy [, ]. |
