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Information on EC 2.1.1.86 - tetrahydromethanopterin S-methyltransferase and Organism(s) Methanosarcina mazei and UniProt Accession P80653

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EC Tree
IUBMB Comments
Involved in the formation of methane from CO2 in methanogenic archaea. The reaction involves the export of one or two sodium ions. The enzyme from the archaeon Methanobacterium thermoautotrophicum is a membrane-associated multienzyme complex composed of eight different subunits, and contains a 5'-hydroxybenzimidazolyl-cobamide prosthetic group, to which the methyl group is attached during the transfer. A soluble enzyme that is induced by the presence of CO has been reported as well .
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Methanosarcina mazei
UNIPROT: P80653 not found.
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Word Map
The taxonomic range for the selected organisms is: Methanosarcina mazei
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
h4mpt, n5-methyltetrahydromethanopterin:coenzyme m methyltransferase, ma4384, mtra-h, tetrahydromethanopterin s-methyltransferase, mtra-h complex, tetrahydromethanopterin methyltransferase, methyl-tetrahydromethanopterin:coenzyme-m methyltransferase, n5-methyltetrahydromethanopterin coenzyme m methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H,MPT:coenzyme M methyltransferase
-
methyltransferase, tetrahydromethanopterin
-
-
-
-
N5-methyltetrahydromethanopterin: coenzyme M methyltransferase
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N5-methyltetrahydromethanopterin:coenzyme M methyltransferase
-
tetrahydromethanopterin methyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
5-methyl-5,6,7,8-tetrahydromethanopterin:coenzyme-M 2-methyltransferase (Na+-transporting)
Involved in the formation of methane from CO2 in methanogenic archaea. The reaction involves the export of one or two sodium ions. The enzyme from the archaeon Methanobacterium thermoautotrophicum is a membrane-associated multienzyme complex composed of eight different subunits, and contains a 5'-hydroxybenzimidazolyl-cobamide prosthetic group, to which the methyl group is attached during the transfer. A soluble enzyme that is induced by the presence of CO has been reported as well [6].
CAS REGISTRY NUMBER
COMMENTARY hide
103406-60-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
show the reaction diagram
methylcobalamin + 2-mercaptoethanesulfonate
?
show the reaction diagram
at 13.6% of the activity compared to 5-methyl-5,6,7,8-tetrahydromethanopterin
-
-
?
N5-methyltetrahydrofolate + 2-mercaptoethanesulfonate
?
show the reaction diagram
at 31.8% of the activity compared to 5-methyl-5,6,7,8-tetrahydromethanopterin
-
-
?
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
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
show the reaction diagram
2-mercaptoethanesulfonate i.e. coenzyme M. The enzyme uses the methylation of coenzyme M (HS-CoM) by methyl-tetrahydromethanopterin to drive an energy-conserving sodium ion pump
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
maximum activity at 1 mM Na+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A0F8JN19_METMZ
240
1
25382
TrEMBL
-
A0A0F8KE09_METMZ
267
8
26942
TrEMBL
-
A0A0F8SHN9_METMZ
250
6
25240
TrEMBL
-
A0A0F8DNF4_METMZ
304
6
32443
TrEMBL
-
A0A0F8EB00_METMZ
250
6
25240
TrEMBL
-
A0A6C0VJW6_METMZ
310
0
33525
TrEMBL
-
A0A0F8MWV6_METMZ
240
1
25366
TrEMBL
-
A0A0F8KKL1_METMZ
72
1
7568
TrEMBL
-
A0A0F8K7P5_METMZ
310
0
33503
TrEMBL
-
A0A0F8LCE3_METMZ
250
6
25226
TrEMBL
-
A0A0F8MB61_METMZ
250
6
25282
TrEMBL
-
A0A0F8MBK2_METMZ
304
6
32489
TrEMBL
-
A0A0F8NNI3_METMZ
108
1
11844
TrEMBL
-
A0A0F8LK40_METMZ
108
1
11872
TrEMBL
-
A0A0F8EG10_METMZ
72
1
8022
TrEMBL
-
A0A0F8IMG8_METMZ
316
0
34058
TrEMBL
-
A0A0F8N613_METMZ
310
0
33477
TrEMBL
-
A0A0F8JQE8_METMZ
316
0
34044
TrEMBL
-
A0A0F8RK79_METMZ
267
8
26972
TrEMBL
-
A0A0F8T6A0_METMZ
197
0
21347
TrEMBL
-
A0A0F8V0B0_METMZ
182
0
19646
TrEMBL
-
A0A4P8QY44_METMZ
74
1
7827
TrEMBL
-
A0A0F8PTP8_METMZ
250
6
25249
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
13000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
20000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
28000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
34000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
380000
non-denaturing gradient PAGE
9000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
during purification, the enzyme is stabilized with 0.01 mM hydroxocobalamin
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
all of these subunits are shown to be heterologously expressed in minicells of the Escherichia coli mutant DK6. Sequence comparisons with the methyltransferases of thermophilic and hypothermophilic methanogenic archaea
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lienard, T.; Becher, B.; Marschall, M.; Bowien, S.; Gottschalk, G.
Sodium ion translocation by N5-methyltetrahydromethanopterin: coenzyme M methyltransferase from Methanosarcina mazei G1 reconstituted in ether lipid liposomes
Eur. J. Biochem.
239
857-864
1996
Methanosarcina mazei (P80655 and P80653 and P80651 and P80654 and P80656 and P80650), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (P80655 and P80653 and P80651 and P80654 and P80656 and P80650)
Manually annotated by BRENDA team
Lienard, T.; Gottschalk, G.
Cloning, sequencing and expression of the genes encoding the sodium translocating N5-methyltetrahydromethanopterin: coenzyme M methyltransferase of the methylotrophic archaeon Methanosarcina mazei G1
FEBS Lett.
425
204-208
1998
Methanosarcina mazei (O59640 and P80655 and O59638 and P80653 and P80651 and P80654 and P80656 and P80650), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (O59640 and P80655 and O59638 and P80653 and P80651 and P80654 and P80656 and P80650)
Manually annotated by BRENDA team