KEGG   ENZYME: 2.8.4.1Help
Entry
EC 2.8.4.1                  Enzyme                                 

Name
coenzyme-B sulfoethylthiotransferase;
methyl-CoM reductase;
methyl coenzyme M reductase
Class
Transferases;
Transferring sulfur-containing groups;
Transferring alkylthio groups
BRITE hierarchy
Sysname
methyl-CoM:CoB S-(2-sulfoethyl)thiotransferase
Reaction(IUBMB)
methyl-CoM + CoB = CoM-S-S-CoB + methane [RN:R04541]
Reaction(KEGG)
Substrate
methyl-CoM [CPD:C03920];
CoB [CPD:C04628]
Product
CoM-S-S-CoB [CPD:C04832];
methane [CPD:C01438]
Comment
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.
History
EC 2.8.4.1 created 2001, modified 2011
Pathway
ec00680  Methane metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K00399  methyl-coenzyme M reductase alpha subunit
K00401  methyl-coenzyme M reductase beta subunit
K00402  methyl-coenzyme M reductase gamma subunit
Genes
MJA: MJ_0081 MJ_0082 MJ_0083 MJ_0842 MJ_0845 MJ_0846
MFE: Mefer_0934 Mefer_0937 Mefer_0938
MVU: Metvu_0145 Metvu_0148 Metvu_0149 Metvu_1192 Metvu_1193 Metvu_1194
MFS: MFS40622_0424 MFS40622_0425 MFS40622_0426 MFS40622_1315 MFS40622_1316 MFS40622_1319
MIF: Metin_0281 Metin_0282 Metin_0285
MJH: JH146_0503 JH146_0504 JH146_0505 JH146_1056 JH146_1057 JH146_1060
MIG: Metig_0442 Metig_0444 Metig_0445 Metig_1233 Metig_1236 Metig_1237
MMP: MMP1555(mcrB) MMP1558(mcrG) MMP1559(mcrA)
MMQ: MmarC5_0017 MmarC5_0018 MmarC5_0021
MMX: MmarC6_1111 MmarC6_1112 MmarC6_1115
MWO: MWSIV6_1521(mrtA) MWSIV6_1522(mrtG) MWSIV6_1524(mrtB) MWSIV6_1556(mcrA) MWSIV6_1557(mcrG) MWSIV6_1560(mcrB)
MST: Msp_0318(mrtB) Msp_0320(mrtG) Msp_0321(mrtA)
MRU: mru_1924(mcrA) mru_1925(mcrG) mru_1928(mcrB)
MEB: Abm4_1526(mcrA) Abm4_1527(mcrG) Abm4_1530(mcrB)
MMIL: sm9_1353(mrtA) sm9_1354(mrtG) sm9_1356(mrtB) sm9_2027(mcrA) sm9_2028(mcrG) sm9_2031(mcrB)
METH: MBMB1_1682(mcrA) MBMB1_1683(mcrG) MBMB1_1686(mcrB) MBMB1_1822(mrtB) MBMB1_1824(mrtG) MBMB1_1825(mrtA)
MFC: BRM9_0935(mcrA) BRM9_0936(mcrG) BRM9_0939(mcrB) BRM9_2153(mrtB) BRM9_2155(mrtG) BRM9_2156(mrtA)
MCUB: MCBB_1985(mcrA) MCBB_1986(mcrG) MCBB_1989(mcrB)
MKA: MK0651(mcrB) MK0654(mcrG) MK0655(mcrA)
MEAR: Mpt1_c01980(mcrB) Mpt1_c02000(mrtG) Mpt1_c02010(mcrA)
MBU: Mbur_2417(mcrA) Mbur_2418(mcrG) Mbur_2421(mcrB)
MCJ: MCON_0759(mcrA) MCON_0760(mcrG) MCON_0762(mcrB)
MBG: BN140_1521(mcrA1) BN140_1522(mcrG1) BN140_1524(mcrB1) BN140_1734(mcrB3) BN140_1737(mcrG3) BN140_1738(mcrA3)
MPD: MCP_0512(mcrB) MCP_0515(mcrG) MCP_0516(mcrA)
MEZ: Mtc_0904(mcrB) Mtc_0907(mcrG) Mtc_0908(mcrA)
RCI: RCIX2059(mcrB) RCIX2062(mcrG) RCIX2063(mcrA)
BARC: AOA65_0406(mrtB) AOA65_0407(mcrG) AOA65_0408(mcrA)
BARB: AOA66_1761(mcrA) AOA66_1769(mrtB) AOA66_1770(mcrG)
 » show all
Taxonomy
Reference
1  [PMID:3122735]
  Authors
Bobik TA, Olson KD, Noll KM, Wolfe RS.
  Title
Evidence that the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium.
  Journal
Biochem Biophys Res Commun 149:455-60 (1987)
DOI:10.1016/0006-291X(87)90389-5
Reference
2
  Authors
Ellermann, J., Hedderich, R., Boecher, R. and Thauer, R.K.
  Title
The final step in methane formation: investigations with highly purified methyl coenzyme M reductase component C from Methanobacterium thermoautotrophicum (strain Marburg).
  Journal
Eur J Biochem 184:63-68 (1988)
Reference
3  [PMID:9367957]
  Authors
Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK.
  Title
Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.
  Journal
Science 278:1457-62 (1997)
DOI:10.1126/science.278.5342.1457
  Sequence
Reference
4  [PMID:11072815]
  Authors
Signor L, Knuppe C, Hug R, Schweizer B, Pfaltz A, Jaun B.
  Title
Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate--a process mimicking methanogenesis in archaea.
  Journal
Chemistry 6:3508-16 (2000)
Reference
5  [PMID:20520712]
  Authors
Scheller S, Goenrich M, Boecher R, Thauer RK, Jaun B
  Title
The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane.
  Journal
Nature 465:606-8 (2010)
DOI:10.1038/nature09015
Other DBs
ExplorEnz - The Enzyme Database: 2.8.4.1
IUBMB Enzyme Nomenclature: 2.8.4.1
ExPASy - ENZYME nomenclature database: 2.8.4.1
UM-BBD (Biocatalysis/Biodegradation Database): 2.8.4.1
BRENDA, the Enzyme Database: 2.8.4.1

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