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Information on EC 2.8.4.1 - coenzyme-B sulfoethylthiotransferase and Organism(s) Methanosarcina barkeri and UniProt Accession P07955

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EC Tree
IUBMB 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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This record set is specific for:
Methanosarcina barkeri
UNIPROT: P07955 not found.
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Word Map
The taxonomic range for the selected organisms is: Methanosarcina barkeri
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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 I
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isoform
MCR I alpha
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MCR I beta
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MCR I gamma
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MCR II
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isoform
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 A
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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 hide
ORGANISM
UNIPROT
LITERATURE
methyl-CoM + CoB = CoM-S-S-CoB + methane
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfo ethyl group transfer
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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 hide
53060-41-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
show the reaction diagram
ethyl-CoM + CoB
CoM-S-S-CoB + ethane
show the reaction diagram
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?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
show the reaction diagram
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
show the reaction diagram
methyl-CoM + CoB
CoM-S-S-CoB + methane
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
CH3-S-CoM + HS-CoB
CoM-S-S-CoB + methane
show the reaction diagram
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MCR catalyzes the methane-forming step in methanogenic archaea
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?
methyl coenzyme M + coenzyme B
methane + CoM-S-S-CoB
show the reaction diagram
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the enzyme catalyzes the final step in methanogenesis
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methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)
methane + CoM-S-S-CoB
show the reaction diagram
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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
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme F430
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2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme
F-430
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A0A8J820_METBA
245
0
26005
TrEMBL
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Q9HHA9_METBA
243
0
27050
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
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alpha2beta2gamma2
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
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methylation of residues in the active site, e.g. at His257, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, 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. The electron density at 1.6 A resolution of the Methanosarcina barkeri enzyme reveals that four of the modified amino acid residues of enzyme from Methanopyrus thermoautotrophicum, namely a thiopeptide, an S-methylcysteine, a 1-N-methylhistidine and a 5-methylarginine are also present. Crystals of the enzyme from Methanosarcina barkeri are grown using a reservoir condition with PEG 5000 monomethylether as precipitant and glycerol as cryoprotectant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant Strep-tagged enzyme by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of Strep-tagged enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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identifying methanotrophic archaea with mcrA sequences
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gunsalus, R.P.; Wolfe, R.S.
Methyl coenzyme M reductase from Methanobacterium thermoautotrophicum. Resolution and properties of the components
J. Biol. Chem.
255
1891-1895
1980
Methanosarcina barkeri, Methanobacterium bryantii, Methanobacterium formicicum, Methanothermobacter thermautotrophicus, Methanospirillum hungatei, no activity in Methanobrevibacter ruminantium, no activity in Methanobrevibacter ruminantium M-1
Manually annotated by BRENDA team
Hallam, S.J.; Girguis, P.R.; Preston, C.M.; Richardson, P.M.; DeLong, E.F.
Identification of methyl coenzyme M reductase A (mcrA) genes associated with methane-oxidizing archaea
Appl. Environ. Microbiol.
69
5483-5491
2003
Methanosarcina barkeri, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Methanospirillum hungatei
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Wagner, T.; Kahnt, J.; Ermler, U.; Shima, S.
Didehydroaspartate modification in methyl-coenzyme M reductase catalyzing methane formation
Angew. Chem. Int. Ed. Engl.
55
10630-10633
2016
Methanosarcina barkeri, Methanothermobacter wolfeii, Methanothermobacter marburgensis
Manually annotated by BRENDA team
Scheller, S.; Goenrich, M.; Thauer, R.K.; Jaun, B.
Methyl-coenzyme M reductase from methanogenic archaea: isotope effects on label exchange and ethane formation with the homologous substrate ethyl-coenzyme M
J. Am. Chem. Soc.
135
14985-14995
2013
Methanosarcina barkeri
Manually annotated by BRENDA team
Nayak, D.; Mahanta, N.; Mitchell, D.; Metcalf, W.
Post-translational thioamidation of methyl-coenzyme M reductase, a key enzyme in methanogenic and methanotrophic Archaea
eLife
6
e29218
2017
Methanosarcina barkeri (P07962 and P07955 and P07964), Methanosarcina acetivorans (Q8THH1 AND Q8THG7 AND Q8THH0), Methanosarcina acetivorans, Methanosarcina acetivorans ATCC 35395 (Q8THH1 AND Q8THG7 AND Q8THH0), Methanosarcina barkeri Fusaro (P07962 and P07955 and P07964), Methanosarcina acetivorans DSM 2834 (Q8THH1 AND Q8THG7 AND Q8THH0), Methanosarcina acetivorans JCM 12185 (Q8THH1 AND Q8THG7 AND Q8THH0), Methanosarcina barkeri DSM 804 (P07962 and P07955 and P07964)
Manually annotated by BRENDA team