EC Number   |
General Information |
Reference |
|---|
    4.1.1.81 | evolution |
the CobD protein from Methanosarcina mazei differs from other CobD homologues by the presence of a 111-amino acid cysteine-rich extended C-terminus (MmCobD386-497) annotated as a putative metal-binding domain or zinc finger protein, but it actually is a ferroprotein. This C-terminal domain is sometimes encoded as an independent protein and other times fused to other Cba biosynthetic proteins (e.g. CbiZ, CbiA, CbiH, or BtuC) |
-, 760602 |
| 4.1.1.81 | malfunction |
there is a 2600fold decrease in catalytic efficiency (kcat/Km) when the C-terminus is removed, or a 1200fold decrease when the enzyme is purified normoxically |
-, 760602 |
| 4.1.1.81 | more |
MmCobD displays redox-sensitivity |
-, 760602 |
| 4.1.1.81 | physiological function |
CobD is able to complement a Salmonella enterica CobD mutant |
-, 747153 |
| 4.1.1.81 | physiological function |
MmCobD is a bifunctional enzyme with L-threonine (L-Thr) kinase (PduX, EC 2.7.1.177) and pyridoxal 5'-phosphate (PLP)-dependent L-threonine phosphate (L-Thr-P) decarboxylase activities needed to synthesize the (R)-1-amino-propan-2-ol O-phosphate (a.k.a. (R)-1-amino-2-propanol-O-2-phosphate, AP-P) moiety of cobalamin (Cbl) |
-, 760602 |
| 4.1.1.81 | physiological function |
the product of the SMUL_1544 gene complements a Salmonella enterica CobD mutant lacking an L-threonine-O-3-phosphate decarboxylase |
-, 748104 |
