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Information on EC 2.1.1.250 - trimethylamine-corrinoid protein Co-methyltransferase and Organism(s) Methanosarcina barkeri and UniProt Accession O93658

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EC Tree
IUBMB Comments
The enzyme, which catalyses the transfer of a methyl group from trimethylamine to a trimethylamine-specific corrinoid protein (MttC), is involved in methanogenesis from trimethylamine. The enzyme contains the unusual amino acid pyrrolysine . 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. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
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Methanosarcina barkeri
UNIPROT: O93658
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The taxonomic range for the selected organisms is: Methanosarcina barkeri
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
hide
trimethylamine
+
a [Co(I) trimethylamine-specific corrinoid protein]
=
a [methyl-Co(III) trimethylamine-specific corrinoid protein]
+
dimethylamine
+
a [Co(I) trimethylamine-specific corrinoid protein]
=
a [methyl-Co(III) trimethylamine-specific corrinoid protein]
+
Synonyms
trimethylamine methyltransferase, mv8460, dsy3156 protein, trimethylamine-corrinoid protein co-methyltransferase, non-pyrrolysine mttb homolog, tma methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TMA methyltransferase
-
TMA:CoM methyltransferase
-
trimethylamine methyltransferase
-
SYSTEMATIC NAME
IUBMB Comments
trimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase
The enzyme, which catalyses the transfer of a methyl group from trimethylamine to a trimethylamine-specific corrinoid protein (MttC), is involved in methanogenesis from trimethylamine. The enzyme contains the unusual amino acid pyrrolysine [2]. 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. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
53414-88-3
methylcobalamin-coenzyme M methyltransferase, EC 2.1.1.246 to EC 2.1.1.253
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
trimethylamine + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
show the reaction diagram
-
-
-
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
show the reaction diagram
-
-
-
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
trimethylamine + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
show the reaction diagram
-
-
-
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
show the reaction diagram
-
-
-
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
show the reaction diagram
-
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
RamA
a 60-kDa monomeric iron sulfur protein, is a protein required for reductive activation of corrinoid-dependent methylamine methyltransferase reactions in methanogenic archaea, it is required for in vitro ATP-dependent reductive activation of trimethylamine:CoM methyl transfer mediating the ATP-dependent reductive activation of Co(II) corrinoid to the Co(I) state for the trimethylamine corrinoid protein, MttC, overview
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
the enzyme is involved in the corrinoid-dependent demethylation of methylamines, which are used for coenzyme M methylation
additional information
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MTTB_METBA
495
0
53855
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
mass spectrometric structure analysis, overview, primary structure of MttB
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme as the MttB-MttC complex by repeated gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mttB, co-transcription with gene mtbB1 encoding the DMA methyltransferase. The genes, organized on the chromosome in the order mtbC, mttB, mttC, mttP, and mtbB1, form a single transcriptional unit. The genes of all methyltransferases each contain a single in-frame amber codon
gene mttB, single gene
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krzycki, J.
Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases
Curr. Opin. Chem. Biol.
8
484-491
2004
Methanosarcina barkeri (O93658)
Manually annotated by BRENDA team
Paul, L.; Ferguson Jr., D.; Krzycki, J.
The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons
J. Bacteriol.
182
2520-2529
2000
Methanosarcina barkeri (O93658), Methanosarcina barkeri, Methanosarcina thermophila (Q9P995), Methanosarcina thermophila
Manually annotated by BRENDA team
Soares, J.; Zhang, L.; Pitsch, R.; Kleinholz, N.; Jones, R.; Wolff, J.; Amster, J.; Green-Church, K.; Krzyck, J.
The residue mass of L-pyrrolysine in three distinct methylamine methyltransferases
J. Biol. Chem.
280
36962-36969
2005
Methanosarcina barkeri (O93658), Methanosarcina barkeri MS / DSM 800 (O93658)
Manually annotated by BRENDA team
Ferguson, T.; Soares, J.; Lienard, T.; Gottschalk, G.; Krzycki, J.
RamA, a protein required for reductive activation of corrinoid-dependent methylamine methyltransferase reactions in methanogenic archaea
J. Biol. Chem.
284
2285-2295
2009
Methanosarcina barkeri (O93658)
Manually annotated by BRENDA team