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Information on EC 2.1.1.250 - trimethylamine-corrinoid protein Co-methyltransferase
for references in articles please use BRENDA:EC2.1.1.250
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.250 trimethylamine-corrinoid protein Co-methyltransferase
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.
The expected taxonomic range for this enzyme is: Archaea, Bacteria
- 2.1.1.250
-
methanogen
- methane
-
cobialamin
-
eubacterium
- limosum
- microbiome
-
acetogens
- methyltransferases
-
methanogenesis
-
wood-ljungdahl
- demethylase
- monomethylamine
- hafniense
-
symbionts
- tetrahydrofolate
- methanococcoides
-
amber
-
desulfitobacterium
Reaction Schemes
show+
=
+
+
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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DSY3156 protein
glycine betaine:cob(I)alamin methyltransferase
MMA methyltransferase 1
MMA methyltransferase 2
MtgB
MttB
mttB1C1
mttB2C2
MV8460
MV8460 GB:cob(I)alamin
non-pyrrolysine MttB homolog
nonpyrrolysine MttB homolog
TMA methyltransferase
trimethylamine methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] = a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
methanogenesis from trimethylamine
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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.
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CAS REGISTRY NUMBER
COMMENTARY
53414-88-3
methylcobalamin-coenzyme M methyltransferase, EC 2.1.1.246 to EC 2.1.1.253
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trimethylamine + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
glycine betaine + cob(I)alamin
dimethylglycine + methylcob(III)alamin
Substrates: -
Products: -
Products: -
?
glycine betaine + cob(I)alamin
dimethylglycine + methylcob(III)alamin
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
Methanosarcina barkeri MS / DSM 800
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
-
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
-
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
-
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Substrates: the TMA methyltransferase cognate corrinoid protein MttC
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Substrates: the TMA methyltransferase cognate corrinoid protein MttC
Products: -
Products: -
?
additional information
?
-
Substrates: ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
Products: -
Products: -
?
additional information
?
-
-
Substrates: ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
Products: -
Products: -
?
additional information
?
-
Substrates: ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme MV8460 shows GB:cob(I)alamin methyl-transfer activity. Molecular docking
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme MV8460 shows GB:cob(I)alamin methyl-transfer activity. Molecular docking
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme MV8460 shows GB:cob(I)alamin methyl-transfer activity. Molecular docking
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trimethylamine + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
Methanosarcina barkeri MS / DSM 800
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
-
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
-
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
-
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
Products: -
Products: -
?
additional information
?
-
-
Substrates: ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
Products: -
Products: -
?
additional information
?
-
Substrates: ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
the enzyme belongs to the COG5598 MttB superfamily. Based on the draft B1d genome, MV8460 is the sole Pyl-lacking MttB found in B1d, which is 65% identical and has 83% sequence similarity to Desulfitobacterium hafniense Y51 DhMtgB. Four predicted active site residues may interact with GB as they are conserved between DhMtgB and MV8460: Y94, N199, R309, and H345
evolution
-
the enzyme belongs to the COG5598 MttB superfamily. Based on the draft B1d genome, MV8460 is the sole Pyl-lacking MttB found in B1d, which is 65% identical and has 83% sequence similarity to Desulfitobacterium hafniense Y51 DhMtgB. Four predicted active site residues may interact with GB as they are conserved between DhMtgB and MV8460: Y94, N199, R309, and H345
-
evolution
-
the enzyme belongs to the COG5598 MttB superfamily. Based on the draft B1d genome, MV8460 is the sole Pyl-lacking MttB found in B1d, which is 65% identical and has 83% sequence similarity to Desulfitobacterium hafniense Y51 DhMtgB. Four predicted active site residues may interact with GB as they are conserved between DhMtgB and MV8460: Y94, N199, R309, and H345
-
metabolism
biochemistry of methane formation by Methanosarcina species from monomethylamine, dimethylamine, and trimethylamine: methanogenesis from these substrates is initiated by three methyltransferases that specifically methylate their cognate corrinoid proteins with one of these methylamines, cf. EC 2.1.1.248 and EC 2.1.1.249, overview
metabolism
archaeal methane formation from methylamines is initiated by distinct methyltransferases with specificity for monomethylamine, dimethylamine, or trimethylamine. Each methylamine methyltransferase methylates a cognate corrinoid protein, which is subsequently demethylated by a second methyltransferase to form methyl-coenzyme M, the direct methane precursor
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
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
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
-
the enzyme is involved in the the glycine betaine-dependent methylotrophic methanogenesis pathway. Environmentally abundant quaternary amines (QAs) are a primary source for methanogenesis. The methanogenic archaeon Methanolobus vulcani B1d metabolizes glycine betaine (GB) through a corrinoid-dependent GB:coenzyme M (CoM) methyl transfer pathway
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
-
the enzyme is involved in the the glycine betaine-dependent methylotrophic methanogenesis pathway. Environmentally abundant quaternary amines (QAs) are a primary source for methanogenesis. The methanogenic archaeon Methanolobus vulcani B1d metabolizes glycine betaine (GB) through a corrinoid-dependent GB:coenzyme M (CoM) methyl transfer pathway
-
metabolism
-
the enzyme is involved in the the glycine betaine-dependent methylotrophic methanogenesis pathway. Environmentally abundant quaternary amines (QAs) are a primary source for methanogenesis. The methanogenic archaeon Methanolobus vulcani B1d metabolizes glycine betaine (GB) through a corrinoid-dependent GB:coenzyme M (CoM) methyl transfer pathway
-
physiological function
the enzyme is involved in the corrinoid-dependent demethylation of methylamines, which are used for coenzyme M methylation
physiological function
one of three non-Pyl MttBs in the organism is indeed a corrinoid-dependent methyltransferase, but with specificity for glycine betaine
physiological function
-
MV8460 catalyzes GB-dependent methylation of free cob(I) alamin indicating it is an authentic MtgB enzyme
physiological function
-
one of three non-Pyl MttBs in the organism is indeed a corrinoid-dependent methyltransferase, but with specificity for glycine betaine
-
physiological function
-
MV8460 catalyzes GB-dependent methylation of free cob(I) alamin indicating it is an authentic MtgB enzyme
-
physiological function
-
MV8460 catalyzes GB-dependent methylation of free cob(I) alamin indicating it is an authentic MtgB enzyme
-
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
additional information
Methanosarcina barkeri MS / DSM 800
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MTTB_METBA
495
0
53855
Swiss-Prot
other Location (Reliability: 5)
MTTB_METBF
Methanosarcina barkeri (strain Fusaro / DSM 804)
495
0
53900
Swiss-Prot
Secretory Pathway (Reliability: 2)
MTTB2_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
495
0
53910
Swiss-Prot
-
MTTB1_METMA
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
495
0
53853
Swiss-Prot
-
MTTB_METBU
Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
497
0
53950
Swiss-Prot
-
MTTB_DESHD
Desulfitobacterium hafniense (strain DSM 10664 / DCB-2)
496
0
53572
Swiss-Prot
-
MTTB_DESHY
Desulfitobacterium hafniense (strain Y51)
496
0
53572
Swiss-Prot
-
MTTB2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
495
0
54078
Swiss-Prot
-
MTTB1_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
495
0
53838
Swiss-Prot
-
A0A099SZ42_METMT
333
0
36179
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0E3HAB0_METTE
495
0
53902
TrEMBL
-
A0A0E3NBG9_METTT
Methanosarcina thermophila (strain ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1)
495
0
53902
TrEMBL
Mitochondrion (Reliability: 5)
A0A0E3Q2X7_9EURY
495
0
53923
TrEMBL
other Location (Reliability: 5)
A0A0E3QQH4_METBA
495
0
53900
TrEMBL
Chloroplast (Reliability: 2)
A0A0E3RM75_METMZ
495
0
53856
TrEMBL
Chloroplast (Reliability: 5)
A0A0E3RZX7_METMZ
495
0
53910
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0E3S452_9EURY
495
0
54066
TrEMBL
-
A0A0E3SI84_9EURY
495
0
53839
TrEMBL
-
A0A0E3S992_9EURY
495
0
54036
TrEMBL
-
A0A0E3ST48_METMT
498
0
54125
TrEMBL
other Location (Reliability: 2)
A0A0E3WQT7_METMZ
495
0
53856
TrEMBL
Secretory Pathway (Reliability: 4)
A0A147JW20_HADYE
485
0
53683
TrEMBL
other Location (Reliability: 1)
A0A147JZW2_HADYE
483
0
53814
TrEMBL
other Location (Reliability: 2)
A0A1D8S6B5_9EURY
485
0
53028
TrEMBL
-
A0A1H3ERV4_9EURY
484
0
51148
TrEMBL
other Location (Reliability: 2)
A0A1H6J9C4_9EURY
484
0
51337
TrEMBL
other Location (Reliability: 2)
A0A1I4T343_9EURY
496
0
53791
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1I6XF85_METTE
333
0
36195
TrEMBL
Secretory Pathway (Reliability: 3)
A0A1L3Q291_9EURY
333
0
36534
TrEMBL
other Location (Reliability: 3)
A0A1L9C3D6_9EURY
496
0
54407
TrEMBL
-
A0A1Q6DVN7_METT1
470
0
52116
TrEMBL
other Location (Reliability: 4)
A0A1X7NLV3_9EURY
496
0
54460
TrEMBL
other Location (Reliability: 1)
A0A2A2HVM7_9EURY
333
0
36078
TrEMBL
other Location (Reliability: 2)
A0A2D3C4B4_9EURY
333
0
36476
TrEMBL
Mitochondrion (Reliability: 4)
A0A343TG99_9EURY
485
0
53164
TrEMBL
other Location (Reliability: 1)
A0A8J8PHV4_9ARCH
333
0
36435
TrEMBL
other Location (Reliability: 2)
A0AA96V9A9_9EURY
334
0
36164
TrEMBL
other Location (Reliability: 1)
A0AA96VFM0_9EURY
334
0
36023
TrEMBL
other Location (Reliability: 1)
A0AA96VBZ4_9EURY
334
0
36059
TrEMBL
Secretory Pathway (Reliability: 1)
D5E7N9_METMS
Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP)
333
0
36429
TrEMBL
-
D7EAB0_METEZ
Methanohalobium evestigatum (strain ATCC BAA-1072 / DSM 3721 / NBRC 107634 / OCM 161 / Z-7303)
495
0
54794
TrEMBL
other Location (Reliability: 5)
F7XPR3_METZD
Methanosalsum zhilinae (strain DSM 4017 / NBRC 107636 / OCM 62 / WeN5)
333
0
36408
TrEMBL
-
L0KUI1_METHD
Methanomethylovorans hollandica (strain DSM 15978 / NBRC 107637 / DMS1)
496
0
54231
TrEMBL
-
M1QA78_METMZ
333
0
36170
TrEMBL
other Location (Reliability: 2)
M9SDS7_METAX
Methanomethylophilus alvi (strain Mx1201)
504
0
55304
TrEMBL
-
Q12TQ7_METBU
Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
484
0
53216
TrEMBL
other Location (Reliability: 2)
U5Q1T7_METII
Methanomassiliicoccus intestinalis (strain Issoire-Mx1)
496
0
54127
TrEMBL
-
Q24MI2_DESHY
Desulfitobacterium hafniense (strain Y51)
471
0
51768
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
mass spectrometric structure analysis, overview, primary structure of MttB
additional information
Methanosarcina barkeri MS / DSM 800
-
mass spectrometric structure analysis, overview, primary structure of MttB
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of native protein, bound to substrate analogue sulfite, and in complex with cognate corrinoid protein MttC, to 2.5, 3.2, and 2.7 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the determined N-terminus of MttB, encoded by mttB, shows a UAG codon, which is represented in both strands of the DNA, follows at codon position 334. Cessation of translation at the UAG codon results in a 34-kDa product rather than the abundant 53-kDa polypeptide purified from TMA-grown cells
additional information
-
the determined N-terminus of MttB, encoded by mttB, shows a UAG codon, which is represented in both strands of the DNA, follows at codon position 334. Cessation of translation at the UAG codon results in a 34-kDa product rather than the abundant 53-kDa polypeptide purified from TMA-grown cells
additional information
the determined N-terminus of MttB, encoded by mttB, shows a UAG codon, which is represented in both strands of the DNA, follows at codon position 334. Cessation of translation at the UAG codon results in a 34-kDa product rather than the abundant 53-kDa polypeptide purified from TMA-grown cells
additional information
-
the determined N-terminus of MttB, encoded by mttB, shows a UAG codon, which is represented in both strands of the DNA, follows at codon position 334. Cessation of translation at the UAG codon results in a 34-kDa product rather than the abundant 53-kDa polypeptide purified from TMA-grown cells
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme as the MttB-MttC complex by repeated gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mtgB or MV8460, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
-
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 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
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, 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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is upregulated during growth on glycine betaine
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
the enzyme is upregulated during growth on glycine betaine
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
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
under nitrogen limitation, a 543fold up-regulation of the mtmB2C2 operon, encoding MMA methyltransferase 2, is obtained when methanol is used as carbon source
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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)
brenda
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
brenda
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 (P58974), Methanosarcina mazei (P58973), Methanosarcina mazei Goe1 (P58974), Methanosarcina mazei Goe1 (P58973)
brenda
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)
brenda
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)
brenda
Ticak, T.; Kountz, D.J.; Girosky, K.E.; Krzycki, J.A.; Ferguson, D.J.
A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase
Proc. Natl. Acad. Sci. USA
111
E4668-E4676
2014
Desulfitobacterium hafniense (Q24MI2), Desulfitobacterium hafniense, Desulfitobacterium hafniense Y51 (Q24MI2)
brenda
Creighbaum, A.J.; Ticak, T.; Shinde, S.; Wang, X.; Ferguson, D.J.
Examination of the glycine betaine-dependent methylotrophic methanogenesis pathway insights into anaerobic quaternary amine methylotrophy
Front. Microbiol.
10
2572
2019
Methanolobus vulcani, Methanolobus vulcani B1d
brenda
Li, J.; Kang, P.T.; Jiang, R.; Lee, J.Y.; Soares, J.A.; Krzycki, J.A.; Chan, M.K.
Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex
Commun. Biol.
6
54
2023
Methanosarcina barkeri (O93658)
brenda
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