Information on EC 2.1.1.90 -

Information on EC 2.1.1.90 - methanol-corrinoid protein Co-methyltransferase:

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EC NUMBER	COMMENTARY
2.1.1.90	-

RECOMMENDED NAME	GeneOntology No.
methanol-corrinoid protein Co-methyltransferase	GO:0047152

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
methanol + a [Co(I) methanol-specific corrinoid protein] = a [methyl-Co(III) methanol-specific corrinoid protein] + H2O		-	-	-	-

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
methyl group transfer	-	-	-	-

PATHWAY	KEGG Link	MetaCyc Link
methanogenesis from methanol	-	CO2FORM-PWY
NIL	-	MTAMBARKMULTI-RXN

SYSTEMATIC NAME

IUBMB Comments

methanol:5-hydroxybenzimidazolylcobamide Co-methyltransferase

The enzyme, which catalyses the transfer of methyl groups from methanol to a methanol-specific corrinoid protein (MtaC), is involved in methanogenesis from methanol. 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. Free cob(I)alamin can substitute for the corrinoid protein in vitro [2]. Inactivated by oxygen and other oxidizing agents, and reactivated by catalytic amounts of ATP and hydrogen.

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
methanol cobalamin methyltransferase	-	-	-	-
methanol:5-hydroxy-benzimidazolylcobamide methyltransferase	Methanosarcina acetivorans	-	-	680470
methanol:5-hydroxybenzimidazolylcobamide methyltransferase	-	-	-	-
methyltransferase, methanol-cobalamin	-	-	-	-
MT 1	-	-	-	-
MtaB	Methanosarcina acetivorans	-	-	680470
MtaB	Methanosarcina barkeri	-	-	682524

CAS REGISTRY NUMBER	COMMENTARY
86611-98-5	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Eubacterium limosum	-	485663	-	-
Methanobacterium bryantii	-	485664	-	-
Methanosarcina acetivorans	strain C2A	680470, 681980, 698630	-	-
Methanosarcina barkeri	-	485660, 485661, 485662, 485665, 485666, 682524	-	-
Methanothermobacter thermautotrophicus	-	485663	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
methanol + 5-hydroxybenzimidazolylcobamide	Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O		Methanosarcina barkeri	-	-	485666	-	485666	-
methanol + 5-hydroxybenzimidazolylcobamide	Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O		Methanosarcina barkeri	-	one of the enzymes responsible for the transmethylation from methanol to coenzyme M	485660	-	485660	?
methanol + 5-hydroxybenzimidazolylcobamide	Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O		Methanosarcina acetivorans	-	methanol catabolism in Methanosarcina species requires the concerted effort of methanol:5-hydroxybenzimidazolylcobamide methyltransferase (MtaB), a corrinoid-containing methyl-accepting protein (MtaC) and Co-methyl-5-hydroxybenzimidazolylcobamide:2-mercapto-ethanesulfonic acid methyltransferase (MtaA). Methanosarcina acetivorans possesses three operons encoding putative methanol-specific MtaB and corrinoid proteins: mtaCB1, mtaCB2 and mtaCB3. Deletion mutants lacking the three operons, in all possible combinations, are constructed and characterized. Strains deleted for any two of the operons grow on methanol, whereas strains lacking all three do not	681980	-	-	?
methanol + cob(I)alamin	methyl-cob(III)alamin + H2O		Methanosarcina barkeri	-	-	485666	-	485666	-
methanol + cob(I)alamin	methyl-cob(III)alamin + H2O		Methanosarcina barkeri	-	catalyzed by beta subunit MtaB alone	485665	-	485665	r
additional information	?	-	Methanosarcina acetivorans	-	analysis of mtaCB gene regulation in Methanosarcina acetivorans	680470	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
methanol + 5-hydroxybenzimidazolylcobamide	Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O		Methanosarcina barkeri	-	one of the enzymes responsible for the transmethylation from methanol to coenzyme M	485660	-	485660
methanol + 5-hydroxybenzimidazolylcobamide	Co-methyl-Co-5-hydroxybenzimidazolylcobamide + H2O		Methanosarcina acetivorans	-	methanol catabolism in Methanosarcina species requires the concerted effort of methanol:5-hydroxybenzimidazolylcobamide methyltransferase (MtaB), a corrinoid-containing methyl-accepting protein (MtaC) and Co-methyl-5-hydroxybenzimidazolylcobamide:2-mercapto-ethanesulfonic acid methyltransferase (MtaA). Methanosarcina acetivorans possesses three operons encoding putative methanol-specific MtaB and corrinoid proteins: mtaCB1, mtaCB2 and mtaCB3. Deletion mutants lacking the three operons, in all possible combinations, are constructed and characterized. Strains deleted for any two of the operons grow on methanol, whereas strains lacking all three do not	681980	-	-
additional information	?	-	Methanosarcina acetivorans	-	analysis of mtaCB gene regulation in Methanosarcina acetivorans	680470	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
5-Hydroxybenzimidazolylcobamide	Methanosarcina barkeri	-	3-4 molecules bound, acting as methyl acceptor	485660	2D-image
5-Hydroxybenzimidazolylcobamide	Methanosarcina barkeri	-	-	485662	2D-image
5-Hydroxybenzimidazolylcobamide	Methanosarcina barkeri	-	corrinoid protein	485666	2D-image

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Ba2+	Methanosarcina barkeri	-	metal-free enzyme preparation has no activity, addition of Ba2+ restores 27% of the original activity	485660
Ca2+	Methanosarcina barkeri	-	metal-free enzyme preparation has no activity, addition of Ca2+ restores 35% of the original activity	485660
Co2+	Methanosarcina barkeri	-	metal-free enzyme preparation has no activity, addition of Co+ restores 46% of the original activity	485660
Mg2+	Methanosarcina barkeri	-	metal-free enzyme preparation has no activity, addition of Mg2+ restores 66% of the original activity	485660
Mn2+	Methanosarcina barkeri	-	metal-free enzyme preparation has no activity, addition of Mn2+ restores 27% of the original activity	485660
Ni2+	Methanosarcina barkeri	-	metal-free enzyme preparation has no activity, addition of Ni2+ restores 21% of the original activity	485660
Sr2+	Methanosarcina barkeri	-	metal-free enzyme preparation has no activity, addition of Sr2+ restores 20% of the original activity	485660
Zn2+	Methanosarcina barkeri	-	beta subunit MtaB contains 1 mol Zn2+/mol subunit, Zn2+ can be substituted by Co2+	485665

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
HgCl2	Methanosarcina barkeri	-	1 mM, 90% inhibition	485660	2D-image
Na2SO3	Methanosarcina barkeri	-	1 mM, 50% inhibition	485660	2D-image
NaNO2	Methanosarcina barkeri	-	0.1 mM, 90% inhibition	485660	2D-image
NH4Cl	Methanosarcina barkeri	-	400 mM, 93% inhibition	485660	2D-image
O2	Methanosarcina barkeri	-	inactivation by O2 and other oxidizing agents	485660	2D-image
pyridoxal 5'-phosphate	Methanosarcina barkeri	-	1 mM, 74% inhibition	485660	2D-image

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
ATP	Methanosarcina barkeri	-	half-maximal activation at 0.16 mM ATP	485660	2D-image
additional information	Methanosarcina barkeri	-	reductive activation by a mixture of H2, ferredoxin and hydrogenase but also by CO, ATP, GTP or CTP needed in the reductive activation process; reductive activation by a mixture of H2, ferredoxin needed in the reductive activation process	485660	-
additional information	Methanosarcina barkeri	-	reductive activation by a mixture of H2, ferredoxin needed in the reductive activation process	485661	-

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
40	-	methanol	Methanosarcina barkeri	-	beta subunit MtaB	485665	2D-image

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
750	-	Methanosarcina barkeri	-	-	485666

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7.2	-	Methanosarcina barkeri	-	assay at	485660

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
37	-	Methanosarcina barkeri	-	assay at	485660

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
No entries in this field

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
No entries in this field

PDB	SCOP	CATH	ORGANISM
2i2x, download	SCOP (2i2x)	CATH (2i2x)	Methanosarcina barkeri (strain Fusaro / DSM 804)

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
122000	-	Methanosarcina barkeri	-	PAGE with different gel concentrations	485660

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
trimer	Methanosarcina barkeri	-	alpha2,beta, 2 * 34000 + 1 * 53000, SDS-PAGE in presence of 2-mercaptoethanol	485660
trimer	Methanosarcina barkeri	-	alpha2,beta, 2 * 49000 + 1 * 24000, beta subunit MtaB harbours the corrinoid prosthetic group	485666

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
hanging drop vapor diffusion method, 2.5 A crystal structure of the methanol-activating MtaBC complex from Methanosarcina barkeri composed of the zinc-containing MtaB and the 5-hydroxybenzimidazolylcobamide-carrying MtaC subunits. Crystal structure of this complex organized as a (MtaBC)2 heterotetramer. MtaB folds as a TIM barrel and contains a novel zinc-binding motif. Zinc(II) lies at the bottom of a funnel formed at the C-terminal beta-barrel end and ligates to two cysteinyl sulfurs (Cys-220 and Cys-269) and one carboxylate oxygen (Glu-164)	Methanosarcina barkeri	-	682524

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
presence of divalent cations e.g. Mg2+, Mn2+, Sr2+, Ca2+ or Ba2+ are required for stability	Methanosarcina barkeri	-	485660

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
oxygen-sensitive	Methanosarcina barkeri	-	485660, 485662

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Methanosarcina barkeri	-	485660, 485661, 485666

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Methanosarcina barkeri	-	485666
expression of beta subunit MtaB in Escherichia coli	Methanosarcina barkeri	-	485665

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
methanol-specific methyltransferase MT1 isozymes are encoded by three operons mtaCB1, mtaCB2, and mtaCB3. When expressed from the strong PmtaC1 or PmtaC2 promoter, each of the MtaC and MtaB proteins supports growth and methane production at wild-type levels. In contrast, all mtaCB operons exhibit poorer growth and lower rates of methane production when PmtaC3 controlls their expression. All combinations of MtaC, MtaB, and MtaA can form functional methyltransferase MT1/MT2 complexes. Variations in enzyme activity correlate with differences in protein abundance. The mtaCBA transcripts show different stabilities, which are strongly influenced by the growth substrate	Methanosarcina acetivorans	-	698630

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
485660	Van der Meijden, P.; te Br�mmelstroet, B.W.; Poirot, C.M.; van der Drift, C.; Vogels, G.D.	Purification and properties of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri	J. Bacteriol.	160	629-635	1984	Methanosarcina barkeri	PubMed
485661	Van der Meijden, P.; van der Lest, C.; van der Drift, C.; Vogels, G.D.	Reductive activation of methanol: 5-hydroxybenzimidazolylcobamide methyltransferase of Methanosarcina barkeri	Biochem. Biophys. Res. Commun.	118	760-766	1984	Methanosarcina barkeri	PubMed
485662	Van der Meijden, P.; Heythuysen, H.J.; Pouwels, A.; Houwen, F.; van der Drift, C.; Vogels, G.D.	Methyltransferases involved in methanol conversion by Methanosarcina barkeri	Arch. Microbiol.	134	238-242	1983	Methanosarcina barkeri	PubMed
485663	Van der Meijden, P.; van der Drift, C.; Vogels, G.D.	Methanol conversion in Eubacterium limosum	Arch. Microbiol.	138	360-364	1984	Eubacterium limosum, Methanothermobacter thermautotrophicus	-
485664	Taylor, C.D.; Wolfe, R.S.	A simplified assay for coenzyme M (HSCH2CH2SO3). Resolution of methylcobalamin-coenzyme M methyltransferase and use of sodium borohydride	J. Biol. Chem.	249	4886-4890	1974	Methanobacterium bryantii	PubMed
485665	Sauer, K.; Thauer, R.K.	Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Zinc dependence and thermodynamics of the methanol:cob(I)alamin methyltransferase reaction	Eur. J. Biochem.	249	280-285	1997	Methanosarcina barkeri	PubMed
485666	Sauer, K.; Harms, U.; Thauer, R.K.	Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties, and encoding genes of the corrinoid protein MT1	Eur. J. Biochem.	243	670-677	1997	Methanosarcina barkeri	PubMed
680470	Bose, A.; Pritchett, M.A.; Rother, M.; Metcalf, W.W.	Differential regulation of the three methanol methyltransferase isozymes in Methanosarcina acetivorans C2A	J. Bacteriol.	188	7274-7283	2006	Methanosarcina acetivorans	PubMed
681980	Pritchett, M.A.; Metcalf, W.W.	Genetic, physiological and biochemical characterization of multiple methanol methyltransferase isozymes in Methanosarcina acetivorans C2A	Mol. Microbiol.	56	1183-1194	2005	Methanosarcina acetivorans	PubMed
682524	Hagemeier, C.H.; Krer, M.; Thauer, R.K.; Warkentin, E.; Ermler, U.	Insight into the mechanism of biological methanol activation based on the crystal structure of the methanol-cobalamin methyltransferase complex	Proc. Natl. Acad. Sci. USA	103	18917-18922	2006	Methanosarcina barkeri	PubMed
698630	Opulencia, R.B.; Bose, A.; Metcalf, W.W.	Physiology and posttranscriptional regulation of methanol:coenzyme M methyltransferase isozymes in Methanosarcina acetivorans C2A	J. Bacteriol.	191	6928-6935	2009	Methanosarcina acetivorans	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.90)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

SYSTERS

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

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