|Gene:||mttC||Accession Number: G-9438 (MetaCyc)|
Species: Methanosarcina barkeri
Reconstitution of trimethylamine-dependent coenzyme M (CoM) methylation showed that three polypeptides were involved - trimethylamine--corrinoid protein Co-methyltransferase, trimethylamine-specific corrinoid protein and methylated [methylamine-specific corrinoid protein]:coenzyme M methyltransferase.
The first two proteins, of sizes 52 and 26 kDa, respectively, copurified as a single trimethylamine methyltransferase (TMA-MT). Gel permeation of the TMA-MT fraction demonstrated that the 52- kDa polypeptide eluted with an apparent molecular mass of 280 kDa. The 26-kDa protein eluted primarily as a monomer, but some 26-kDa polypeptides also eluted with the 280-kDa peak, indicating that the two proteins weakly associate [Ferguson97].
Molecular Weight of Polypeptide: 22.949 kD (from nucleotide sequence), 26 kD (experimental) [Ferguson97 ]
Relationship Links: Entrez-Nucleotide:RELATED-TO:AF102623 , InterPro:IN-FAMILY:IPR003759 , InterPro:IN-FAMILY:IPR006158 , InterPro:IN-FAMILY:IPR012741 , Pfam:IN-FAMILY:PF02310 , Pfam:IN-FAMILY:PF02607 , Prosite:IN-FAMILY:PS51332 , Prosite:IN-FAMILY:PS51337 , Smart:IN-FAMILY:SM01018
Reactions known to consume the compound:
Reactions known to produce the compound:
In Reactions of unknown directionality:
Not in pathways:
a [Co(II) trimethylamine-specific corrinoid protein] + ATP + an unknown reduced electron acceptor = a [Co(I) trimethylamine-specific corrinoid protein] + ADP + an unknown oxidized electron acceptor + phosphate
Ferguson97: Ferguson DJ, Krzycki JA (1997). "Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri." J Bacteriol 179(3);846-52. PMID: 9006042
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