EC Number   |
General Information |
Reference |
|---|
   2.1.1.250 | evolution |
the enzyme belongs to the COG5598 MttB superfamily. Based on the draft B1d genome, MV8460 is the sole Pyl-lacking MttB found in B1d, which is 65% identical and has 83% sequence similarity to Desulfitobacterium hafniense Y51 DhMtgB. Four predicted active site residues may interact with GB as they are conserved between DhMtgB and MV8460: Y94, N199, R309, and H345 |
-, 756781 |
| 2.1.1.250 | metabolism |
archaeal methane formation from methylamines is initiated by distinct methyltransferases with specificity for monomethylamine, dimethylamine, or trimethylamine. Each methylamine methyltransferase methylates a cognate corrinoid protein, which is subsequently demethylated by a second methyltransferase to form methyl-coenzyme M, the direct methane precursor |
717781 |
| 2.1.1.250 | metabolism |
biochemistry of methane formation by Methanosarcina species from monomethylamine, dimethylamine, and trimethylamine: methanogenesis from these substrates is initiated by three methyltransferases that specifically methylate their cognate corrinoid proteins with one of these methylamines, cf. EC 2.1.1.248 and EC 2.1.1.249, overview |
717525 |
| 2.1.1.250 | metabolism |
the enzyme is involved in the the glycine betaine-dependent methylotrophic methanogenesis pathway. Environmentally abundant quaternary amines (QAs) are a primary source for methanogenesis. The methanogenic archaeon Methanolobus vulcani B1d metabolizes glycine betaine (GB) through a corrinoid-dependent GB:coenzyme M (CoM) methyl transfer pathway |
-, 756781 |
| 2.1.1.250 | metabolism |
three different methyltransferases initiate methanogenesis from trimethylamine, dimethylamine, or monomethylamine by methylating different cognate corrinoid proteins that are subsequently used to methylate coenzyme M |
717721 |
| 2.1.1.250 | metabolism |
when growing on trimethylamine, nitrogen fixation does not occur in the cells, indicating that ammonium released during trimethylamine degradation is sufficient to serve as a nitrogen source and represses nif gene induction, transcriptional regulation of soluble methyltransferases, which catalyze the initial step of methylamine consumption by methanogenesis, in response to different carbon and nitrogen sources, overview. Transcription of the operon encoding TMA methyltransferase is not regulated in response to the nitrogen source. Regulation of soluble methyltransferases in response to different nitrogen and carbon sources, overview |
-, 717723 |
| 2.1.1.250 | more |
single in-frame amber UAG codons are found in the genes encoding MtmB, MtbB, or MttB, the methyltransferases initiating methane formation from monomethylamine, dimethylamine, or trimethylamine, respectively, in certain Archaea. The amber codon codes for pyrrolysine, the 22nd genetically encoded amino acid found in nature |
-, 717771 |
| 2.1.1.250 | physiological function |
MV8460 catalyzes GB-dependent methylation of free cob(I) alamin indicating it is an authentic MtgB enzyme |
-, 756781 |
| 2.1.1.250 | physiological function |
one of three non-Pyl MttBs in the organism is indeed a corrinoid-dependent methyltransferase, but with specificity for glycine betaine |
-, 737168 |
| 2.1.1.250 | physiological function |
the enzyme is involved in the corrinoid-dependent demethylation of methylamines, which are used for coenzyme M methylation |
717525 |
