KEGG   ENZYME: 2.1.1.247Help
Entry
EC 2.1.1.247                Enzyme                                 

Name
[methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase;
methyltransferase 2 (ambiguous);
MT2 (ambiguous);
MT2-A;
mtbA (gene name)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
methylated monomethylamine-specific corrinoid protein:CoM methyltransferase
Reaction(IUBMB)
a [methyl-Co(III) methylamine-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methylamine-specific corrinoid protein] [RN:R10000]
Reaction(KEGG)
Substrate
[methyl-Co(III) methylamine-specific corrinoid protein];
CoM [CPD:C03576]
Product
methyl-CoM [CPD:C03920];
[Co(I) methylamine-specific corrinoid protein]
Comment
Contains zinc [2]. The enzyme, which is involved in methanogenesis from mono-, di-, and trimethylamine, catalyses the transfer of a methyl group bound to the cobalt cofactor of several corrinoid proteins (mono-, di-, and trimethylamine-specific corrinoid proteins, cf. EC 2.1.1.248, methylamine---corrinoid protein Co-methyltransferase, EC 2.1.1.249, dimethylamine---corrinoid protein Co-methyltransferase, and EC 2.1.1.250, trimethylamine---corrinoid protein Co-methyltransferase) to CoM, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.
History
EC 2.1.1.247 created 2012
Pathway
ec00680  Methane metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K14082  [methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase
Genes
MAC: MA_0146(mtbA)
MBA: Mbar_A0841
MBY: MSBRM_0152
MBW: MSBRW_0160
MBAR: MSBR2_2229
MBAK: MSBR3_2280
MMA: MM_1439(mtbA)
MMAZ: MmTuc01_1497
MMJ: MSMAS_3225
MMAC: MSMAC_3247
MTHE: MSTHC_1355
MTHR: MSTHT_1928
MHOR: MSHOH_3972
MBU: Mbur_2082(mtbA)
MMET: MCMEM_0281
MMH: Mmah_0279
 » show all
Taxonomy
Reference
1  [PMID:7635826]
  Authors
Burke SA, Krzycki JA
  Title
Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine.
  Journal
J Bacteriol 177:4410-6 (1995)
DOI:10.1128/JB.177.15.4410-4416.1995
  Sequence
Reference
2  [PMID:8702528]
  Authors
LeClerc GM, Grahame DA
  Title
Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression.
  Journal
J Biol Chem 271:18725-31 (1996)
DOI:10.1074/jbc.271.31.18725
  Sequence
Reference
3  [PMID:9006042]
  Authors
Ferguson DJ Jr, Krzycki JA
  Title
Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri.
  Journal
J Bacteriol 179:846-52 (1997)
DOI:10.1128/JB.179.3.846-852.1997
  Sequence
Reference
4  [PMID:9642198]
  Authors
Burke SA, Lo SL, Krzycki JA
  Title
Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine.
  Journal
J Bacteriol 180:3432-40 (1998)
  Sequence
Reference
5  [PMID:10852929]
  Authors
Ferguson DJ Jr, Gorlatova N, Grahame DA, Krzycki JA
  Title
Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri.
  Journal
J Biol Chem 275:29053-60 (2000)
DOI:10.1074/jbc.M910218199
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.247
IUBMB Enzyme Nomenclature: 2.1.1.247
ExPASy - ENZYME nomenclature database: 2.1.1.247
BRENDA, the Enzyme Database: 2.1.1.247

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