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Information on EC 2.1.1.250 - trimethylamine-corrinoid protein Co-methyltransferase and Organism(s) Methanosarcina mazei and UniProt Accession P58973

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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 mazei
UNIPROT: P58973
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The taxonomic range for the selected organisms is: Methanosarcina mazei
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, tma methyltransferase, dsy3156 protein, trimethylamine-corrinoid protein co-methyltransferase, non-pyrrolysine mttb homolog, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MMA methyltransferase 1
-
MMA methyltransferase 2
-
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
-
-
-
?
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
-
-
-
?
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
DSM 3647, gene mttB1C1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
when growing on trimethylamine, nitrogen fixation does not occur in the cells, indicating that ammonium released during trimethylamine degradation is sufficient to serve as a nitrogen source and represses nif gene induction, transcriptional regulation of soluble methyltransferases, which catalyze the initial step of methylamine consumption by methanogenesis, in response to different carbon and nitrogen sources, overview. Transcription of the operon encoding TMA methyltransferase is not regulated in response to the nitrogen source. Regulation of soluble methyltransferases in response to different nitrogen and carbon sources, overview
metabolism
when growing on trimethylamine, nitrogen fixation does not occur in the cells, indicating that ammonium released during trimethylamine degradation is sufficient to serve as a nitrogen source and represses nif gene induction, transcriptional regulation of soluble methyltransferases, which catalyze the initial step of methylamine consumption by methanogenesis, in response to different carbon and nitrogen sources, overview. Transcription of the operon encoding TMA methyltransferase is not regulated in response to the nitrogen source. Regulation of soluble methyltransferases in response to different nitrogen and carbon sources, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mttB1C1, operon encoding TMA methylamine methyltransferase, quantitative RT-PCR expression analysis, comparison with other methylamine methyltransferases, overview. Transcriptional regulation of genes encoding methylamine methyltransferases (MT) in cells growing on TMA or methanol in the presence of ammonium, overview
gene mttB2C2, operon encoding TMA methylamine methyltransferase, quantitative RT-PCR expression analysis, comparison with other methylamine methyltransferases, overview. Transcriptional regulation of genes encoding methylamine methyltransferases (MT) in cells growing on TMA or methanol in the presence of ammonium, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription of the mtmB1C1 operon is not affected by the nitrogen source but appears to be increased when trimethylamine is the sole carbon and energy source. Transcription of the homologous mtmB1C1 operon occurs at a constant level independently of the nitrogen source
under nitrogen limitation, a 543fold up-regulation of the mtmB2C2 operon, encoding MMA methyltransferase 2, is obtained when methanol is used as carbon source
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Veit, K.; Ehlers, C.; Schmitz, R.
Effects of nitrogen and carbon sources on transcription of soluble methyltransferases in Methanosarcina mazei strain G1
J. Bacteriol.
187
6147-6154
2005
Methanosarcina mazei (P58973), Methanosarcina mazei (P58974), Methanosarcina mazei Goe1 (P58973), Methanosarcina mazei Goe1 (P58974)
Manually annotated by BRENDA team