KEGG   ENZYME: 2.1.1.382
Entry
EC 2.1.1.382                Enzyme                                 
Name
methoxylated aromatic compound---corrinoid protein Co-methyltransferase;
mtoB (gene name);
mtvB (gene name);
vdmB (gene name)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
methoxylated aromatic compound:cobamide Co-methyltransferase
Reaction(IUBMB)
a methoxylated aromatic compound + a [Co(I) methoxylated-aromatic-compound-specific corrinoid protein] = a [methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein] + a phenol
Reaction(KEGG)
(other) R07668
Substrate
methoxylated aromatic compound;
[Co(I) methoxylated-aromatic-compound-specific corrinoid protein]
Product
[methyl-Co(III) methoxylated-aromatic-compound-specific corrinoid protein];
phenol [CPD:C00146]
Comment
This entry stands for a family of enzymes that have been characterized from acetogenic bacteria and archaeal species. Different members of this family have different substrate specificity. In the methanogenic archaeon Methermicoccus shengliensis the enzyme participates in methanogenesis from methoxylated aromatic compounds, while in acetogenic bacteria and in non-methanogenic archaea it participates in methoxydotrophic growth. Most of the enzymes have a wide specificity and were shown to act on a large number of methoxylated aromatic compounds, carrying a methoxy group at positions 2, 3 or 4 of the aromatic ring. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state; during methylation the cobalt is oxidized to the Co(III) state.
History
EC 2.1.1.382 created 2022
Pathway
ec00627  Aminobenzoate degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K25916  methoxylated aromatic compound---corrinoid protein Co-methyltransferase
Genes
DORDesor_3939
DAIDesaci_1204
DMIDesmer_3053
AACXDEACI_1430
BLARLC508_16885
TPZTph_c09100
MTAMoth_0386 Moth_1317
MTHOMOTHE_c03170 MOTHE_c13020
MTHZMOTHA_c04110 MOTHA_c13880
FPESNXS98_04865
CCOPMal65_31530
AFUAF_0007
AFGAFULGI_00000050
MPIMpet_2558
MOUOU421_04700
MBNMboo_1040
 » show all
Reference
1  [PMID:9654069]
  Authors
Kaufmann F, Wohlfarth G, Diekert G.
  Title
O-demethylase from Acetobacterium dehalogenans--substrate specificity and function of the participating proteins.
  Journal
Eur J Biochem 253:706-11 (1998)
DOI:10.1046/j.1432-1327.1998.2530706.x
Reference
2  [PMID:11409548]
  Authors
Engelmann T, Kaufmann F, Diekert G.
  Title
Isolation and characterization of a veratrol:corrinoid protein methyl transferase from Acetobacterium dehalogenans.
  Journal
Arch Microbiol 175:376-83 (2001)
DOI:10.1007/s002030100275
Reference
3  [PMID:11344134]
  Authors
Naidu D, Ragsdale SW.
  Title
Characterization of a three-component vanillate O-demethylase from Moorella thermoacetica.
  Journal
J Bacteriol 183:3276-81 (2001)
DOI:10.1128/JB.183.11.3276-3281.2001
Reference
4  [PMID:18631365]
  Authors
Pierce E, Xie G, Barabote RD, Saunders E, Han CS, Detter JC, Richardson P, Brettin TS, Das A, Ljungdahl LG, Ragsdale SW
  Title
The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum).
  Journal
Environ Microbiol 10:2550-73 (2008)
DOI:10.1111/j.1462-2920.2008.01679.x
  Sequence
Reference
5  [PMID:34145392]
  Authors
Kurth JM, Nobu MK, Tamaki H, de Jonge N, Berger S, Jetten MSM, Yamamoto K, Mayumi D, Sakata S, Bai L, Cheng L, Nielsen JL, Kamagata Y, Wagner T, Welte CU.
  Title
Methanogenic archaea use a bacteria-like methyltransferase system to demethoxylate aromatic compounds.
  Journal
ISME J 15:3549-3565 (2021)
DOI:10.1038/s41396-021-01025-6
Reference
6  [PMID:33913565]
  Authors
Welte CU, de Graaf R, Dalcin Martins P, Jansen RS, Jetten MSM, Kurth JM.
  Title
A novel methoxydotrophic metabolism discovered in the hyperthermophilic archaeon Archaeoglobus fulgidus.
  Journal
Environ Microbiol 23:4017-4033 (2021)
DOI:10.1111/1462-2920.15546
  Sequence
[afu:AF_0007]
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.382
IUBMB Enzyme Nomenclature: 2.1.1.382
ExPASy - ENZYME nomenclature database: 2.1.1.382
BRENDA, the Enzyme Database: 2.1.1.382

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