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Information on EC 2.1.1.250 - trimethylamine-corrinoid protein Co-methyltransferase and Organism(s) Methanosarcina thermophila and UniProt Accession Q9P995

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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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This record set is specific for:
Methanosarcina thermophila
UNIPROT: Q9P995
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Word Map
The taxonomic range for the selected organisms is: Methanosarcina thermophila
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
+
a [Co(I) trimethylamine-specific corrinoid protein]
=
a [methyl-Co(III) trimethylamine-specific corrinoid protein]
+
Synonyms
trimethylamine methyltransferase, mv8460, tma methyltransferase, dsy3156 protein, trimethylamine-corrinoid protein co-methyltransferase, non-pyrrolysine mttb homolog, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TMA 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) 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) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MttB; gene mttB
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
three different methyltransferases initiate methanogenesis from trimethylamine, dimethylamine, or monomethylamine by methylating different cognate corrinoid proteins that are subsequently used to methylate coenzyme M
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MTTB_METTE
483
0
52555
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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