| Type: | Domain | Name: | Molybdenum cofactor sulfurase, C-terminal-like |
| Description: | Molybdenum cofactor (MOCO) sulphurases [] catalyse the insertion of a terminal sulphur ligand into the molybdenum cofactor, thereby converting the oxo form of MOCO to a sulphurylated form. Suphurylated MOCO is required by several enzymes, including: aldehyde oxidase (), which function in the last step of abscisic acid biosynthesis in plants []; and xanthine dehydrogenase (), which synthesis uric acid from xanthine during nitrogen metabolism [].This entry represents the beta-barrel C-terminal domain of MOCO sulphurase (MOSC domain), which has a beta-barrel structure similar to that of the beta-barrel domain in pyruvate kinase. MOSC domains are found in several proteins from both eukaryotes and prokaryotes, and have a highly conserved cysteine residue required for activity. MOSC domains are found as stand-alone forms, such as the YiiM protein from Escherichia coli, or fused to other domains, such as a NifS-like catalytic domain in MOCO sulphurase. The MOSC domain is predicted to be a sulphur-carrier domain that receives sulphur abstracted from pyridoxal phosphate-dependent NifS-like enzymes, using it for the formation of diverse sulphur-metal clusters []. | Short Name: | MoCF_Sase_C-like |
