MetaCyc Polypeptide: trimethylamine-specific corrinoid protein

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 ]

Unification Links: Protein Model Portal:O93659 , UniProt:O93659

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

Created 25-May-2006 by Caspi R , SRI International


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

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Sat Oct 10, 2015, BIOCYC14A.