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Information on EC 2.8.4.1 - coenzyme-B sulfoethylthiotransferase and Organism(s) Methanopyrus kandleri and UniProt Accession Q49604
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2.8.4.1 coenzyme-B sulfoethylthiotransferaseIUBMB Comments
This enzyme catalyses the final step in methanogenesis, the biological production of methane. This important anaerobic process is carried out only by methanogenic archaea. The enzyme can also function in reverse, for anaerobic oxidation of methane.The enzyme requires the hydroporphinoid nickel complex coenzyme F430. Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates. The sulfide sulfur can be replaced by selenium but not by oxygen.
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Word Map
- 2.8.4.1
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methanogen
- methane
- archaea
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methanogenesis
- nickel
- methanobacterium
- methanosarcina
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methanotrophic
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hydrogenotrophic
- thermoautotrophicum
- ch4
- methanosarcinales
- methanomicrobiales
- methanothermobacter
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sulfate-reducing
- heterodisulfide
- methanobrevibacter
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methane-producing
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seep
- acetivorans
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anme-1
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t-rflp
- methanobacteriales
-
biogas
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phylotypes
- methanosarcinaceae
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nickel-containing
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acetoclastic
- methanosaeta
- marburgensis
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methane-oxidizing
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syntrophic
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methane-forming
- 2-bromoethanesulfonate
- biofuel production
- analysis
- vannielii
- methanoculleus
-
niiii
- methanopyrus
- synthesis
- methanococcales
- hs-com
- environmental protection
- com-s-s-cob
The taxonomic range for the selected organisms is: Methanopyrus kandleri
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Synonyms
methyl-coenzyme m reductase, methyl coenzyme m reductase, methyl-com reductase, methyl coenzyme-m reductase, mcr ii, mcr i, mcrox1, methyl coenzyme m reductase a, methyl-coenzyme-m reductase, methyl-coenzyme m reductase a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-(methylthio)ethanesulfonic acid reductase
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Coenzyme-B sulfoethylthiotransferase alpha
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Coenzyme-B sulfoethylthiotransferase beta
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Coenzyme-B sulfoethylthiotransferase gamma
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MCR
MCR I alpha
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MCR I beta
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MCR I gamma
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MCR II alpha
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MCR II beta
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MCR II gamma
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methyl coenzyme M reductase
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methyl-coenzyme M reductase
methyl-CoM reductase
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methyl-ScoM reductase
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S-methyl-coenzyme M reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
methyl-CoM + CoB = CoM-S-S-CoB + methane
in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, 2-(S)-methylglutamine alpha400, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfo ethyl group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
methyl-CoM:CoB S-(2-sulfoethyl)thiotransferase
This enzyme catalyses the final step in methanogenesis, the biological production of methane. This important anaerobic process is carried out only by methanogenic archaea. The enzyme can also function in reverse, for anaerobic oxidation of methane.The enzyme requires the hydroporphinoid nickel complex coenzyme F430. Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates. The sulfide sulfur can be replaced by selenium but not by oxygen.
CAS REGISTRY NUMBER
COMMENTARY
53060-41-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
MCR catalyzes the methane-forming step in methanogenic archaea
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CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview
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methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
i.e. methyl-SCoM
a the mixed disulfide
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?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea
a the mixed disulfide
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?
methyl-CoM + CoB
CoM-S-S-CoB + methane
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
MCR catalyzes the methane-forming step in methanogenic archaea
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?
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea
a the mixed disulfide
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?
methyl-CoM + CoB
CoM-S-S-CoB + methane
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
coenzyme F430
2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q49605: alpha subunit, Q49601: beta subunit, Q49604: gamma subunit
SwissProt
Q49605: alpha-subunit, Q49601: beta-subunit, Q49604: gamma-subunit
SwissProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
physiological function
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
methylation of residues in the active site, e.g. at His257, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, crystals of the inactive enzyme are obtained with PEG 550 monomethyl ether as precipitant. Diffraction data to 2.7 A resolution are collected from one crystal of methyl-coenzyme M reductase from Methanopyrus kandleri with a completeness of 63%. Due to the low completeness of the data, refinement of the structure is only possible constraining the 2-fold non-crystallographic symmetry of the methyl-coenzyme M reductase molecule. Comparison of crystal structures of methyl-coenzyme M reductase from Methanosarcina barkeri (growth temperature optimum, 37°C), Methanopyrus kandleri (growth temperature optimum, 98°C) and Methanobacterium thermoautotrophicum (growth temperature optimum, 65°C)
the crystal structures of methyl-coenzyme M reductase from Methanosarcina barkeri and Methanopyrus kandleri are determined and compared with the known structure of MCR from Methanobacterium thermoautotrophicum. The active sites of enzyme from Methanosarcina barkeri and Methanopyrus kandleri are almost identical to that of Methanobacterium thermoautotrophicum and predominantly occupied by coenzyme M and coenzyme B. Crystals of the inactive enzyme from Methanopyrus kandleri are obtained by hanging drop method with PEG 550 monomethylether as precipitant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kahnt, J.; Buchenau, B.; Mahlert, F.; Krueger, M.; Shima, S.; Thauer, R.K.
Post-translational modifications in the active site region of methyl-coenzyme M reductase from methanogenic and methanotrophic archaea
FEBS J.
274
4913-4921
2007
Methanocaldococcus jannaschii, Methanococcus voltae, Methanoculleus thermophilus, Methanopyrus kandleri, Methanopyrus kandleri (Q49605), Methanosarcina barkeri, Methanothermobacter marburgensis
Grabarse, W.; Mahlert, F.; Shima, S.; Thauer, R.K.; Ermler, U.
Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation
J. Mol. Biol.
303
329-344
2000
Methanopyrus kandleri (Q49605 and Q49601 and Q49604), Methanopyrus kandleri, Methanopyrus kandleri DSM 6324 (Q49605 and Q49601 and Q49604), Methanosarcina barkeri (P07962 and P07955 and P07964), Methanosarcina barkeri, Methanosarcina barkeri DSM 804 (P07962 and P07955 and P07964)
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Release 2023.1 (January 2023)
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