EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.8.4.1 | 300000 | - |
- |
Methanosarcina barkeri |
2.8.4.1 | 300000 | - |
- |
Methanocaldococcus jannaschii |
2.8.4.1 | 300000 | - |
- |
Methanopyrus kandleri |
2.8.4.1 | 300000 | - |
- |
Methanococcus voltae |
2.8.4.1 | 300000 | - |
- |
Methanoculleus thermophilus |
2.8.4.1 | 300000 | - |
- |
Methanothermobacter marburgensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.8.4.1 | CH3-S-CoM + HS-CoB | Methanosarcina barkeri | MCR catalyzes the methane-forming step in methanogenic archaea | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | Methanocaldococcus jannaschii | MCR catalyzes the methane-forming step in methanogenic archaea | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | Methanococcus voltae | MCR catalyzes the methane-forming step in methanogenic archaea | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | Methanoculleus thermophilus | MCR catalyzes the methane-forming step in methanogenic archaea | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | Methanothermobacter marburgensis | MCR catalyzes the methane-forming step in methanogenic archaea | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | Methanopyrus kandleri | MCR catalyzes the methane-forming step in methanogenic archaea | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | Methanosarcina barkeri | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | Methanocaldococcus jannaschii | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | Methanopyrus kandleri | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | Methanococcus voltae | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | Methanoculleus thermophilus | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | Methanothermobacter marburgensis | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | methane + CoM-S-S-CoB | a the mixed disulfide | ? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.8.4.1 | Methanocaldococcus jannaschii | - |
gene mcrA | - |
2.8.4.1 | Methanocaldococcus jannaschii | - |
isozyme MCR I | - |
2.8.4.1 | Methanococcus voltae | - |
- |
- |
2.8.4.1 | Methanoculleus thermophilus | - |
isozymes MCR I, gene mcrA | - |
2.8.4.1 | Methanoculleus thermophilus | - |
isozyme MCR I | - |
2.8.4.1 | Methanopyrus kandleri | - |
gene mcrA | - |
2.8.4.1 | Methanopyrus kandleri | Q49605 | - |
- |
2.8.4.1 | Methanosarcina barkeri | - |
- |
- |
2.8.4.1 | Methanosarcina barkeri | - |
gene mcrA | - |
2.8.4.1 | Methanothermobacter marburgensis | - |
isozymes MCR I and MCR II, gene mcrA | - |
2.8.4.1 | Methanothermobacter marburgensis | - |
isozymes MCR I and MCR II | - |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
2.8.4.1 | side-chain modification | methylation of residues in the active site, e.g. at His257, 5fold methylation in isozyme MCR I, overview | Methanocaldococcus jannaschii |
2.8.4.1 | side-chain modification | methylation of residues in the active site, e.g. at His257, 5fold methylation in isozyme MCR I, overview | Methanoculleus thermophilus |
2.8.4.1 | side-chain modification | methylation of residues in the active site, e.g. at His257, 5fold methylation in isozyme MCR I, overview | Methanothermobacter marburgensis |
2.8.4.1 | side-chain modification | methylation of residues in the active site, e.g. at His257, overview | Methanosarcina barkeri |
2.8.4.1 | side-chain modification | methylation of residues in the active site, e.g. at His257, overview | Methanococcus voltae |
2.8.4.1 | side-chain modification | methylation of residues in the active site, e.g. at His257, overview | Methanopyrus kandleri |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.8.4.1 | methyl-CoM + CoB = CoM-S-S-CoB + methane | in the active site region of both isozymes, five modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, S-methylcysteine alpha452, 2-(S)-methylglutamine alpha400, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271 | Methanothermobacter marburgensis | |
2.8.4.1 | 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 | Methanocaldococcus jannaschii | |
2.8.4.1 | 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 | Methanopyrus kandleri | |
2.8.4.1 | 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, S-methylcysteine alpha452, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271 | Methanosarcina barkeri | |
2.8.4.1 | 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, S-methylcysteine alpha452, 2-(S)-methylglutamine alpha400, and 1-N-methylhistidine alpha257 | Methanococcus voltae | |
2.8.4.1 | 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, S-methylcysteine alpha452, 2-(S)-methylglutamine alpha400, and 5-(S)-methylarginine alpha271 | Methanoculleus thermophilus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.8.4.1 | CH3-S-CoM + HS-CoB | MCR catalyzes the methane-forming step in methanogenic archaea | Methanosarcina barkeri | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | MCR catalyzes the methane-forming step in methanogenic archaea | Methanocaldococcus jannaschii | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | MCR catalyzes the methane-forming step in methanogenic archaea | Methanococcus voltae | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | MCR catalyzes the methane-forming step in methanogenic archaea | Methanoculleus thermophilus | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | MCR catalyzes the methane-forming step in methanogenic archaea | Methanothermobacter marburgensis | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | MCR catalyzes the methane-forming step in methanogenic archaea | Methanopyrus kandleri | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | 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 | Methanosarcina barkeri | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | 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 | Methanocaldococcus jannaschii | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | 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 | Methanococcus voltae | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | 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 | Methanoculleus thermophilus | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | 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 | Methanothermobacter marburgensis | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | CH3-S-CoM + HS-CoB | 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 | Methanopyrus kandleri | CoM-S-S-CoB + methane | - |
? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | i.e. methyl-SCoM | Methanosarcina barkeri | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | i.e. methyl-SCoM | Methanocaldococcus jannaschii | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | i.e. methyl-SCoM | Methanopyrus kandleri | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | i.e. methyl-SCoM | Methanococcus voltae | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | i.e. methyl-SCoM | Methanoculleus thermophilus | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | i.e. methyl-SCoM | Methanothermobacter marburgensis | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | Methanosarcina barkeri | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | Methanocaldococcus jannaschii | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | Methanopyrus kandleri | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | Methanococcus voltae | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | Methanoculleus thermophilus | methane + CoM-S-S-CoB | a the mixed disulfide | ? | |
2.8.4.1 | methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) | the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea | Methanothermobacter marburgensis | methane + CoM-S-S-CoB | a the mixed disulfide | ? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.8.4.1 | hexamer | alpha2beta2gamma2 | Methanosarcina barkeri |
2.8.4.1 | hexamer | alpha2beta2gamma2 | Methanocaldococcus jannaschii |
2.8.4.1 | hexamer | alpha2beta2gamma2 | Methanopyrus kandleri |
2.8.4.1 | hexamer | alpha2beta2gamma2 | Methanococcus voltae |
2.8.4.1 | hexamer | alpha2beta2gamma2 | Methanoculleus thermophilus |
2.8.4.1 | hexamer | alpha2beta2gamma2 | Methanothermobacter marburgensis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.8.4.1 | MCR | - |
Methanosarcina barkeri |
2.8.4.1 | MCR | - |
Methanocaldococcus jannaschii |
2.8.4.1 | MCR | - |
Methanopyrus kandleri |
2.8.4.1 | MCR | - |
Methanococcus voltae |
2.8.4.1 | MCR | - |
Methanoculleus thermophilus |
2.8.4.1 | MCR | - |
Methanothermobacter marburgensis |
2.8.4.1 | methyl-coenzyme M reductase | - |
Methanosarcina barkeri |
2.8.4.1 | methyl-coenzyme M reductase | - |
Methanocaldococcus jannaschii |
2.8.4.1 | methyl-coenzyme M reductase | - |
Methanopyrus kandleri |
2.8.4.1 | methyl-coenzyme M reductase | - |
Methanococcus voltae |
2.8.4.1 | methyl-coenzyme M reductase | - |
Methanoculleus thermophilus |
2.8.4.1 | methyl-coenzyme M reductase | - |
Methanothermobacter marburgensis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.8.4.1 | 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 | Methanosarcina barkeri | |
2.8.4.1 | 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 | Methanocaldococcus jannaschii | |
2.8.4.1 | 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 | Methanopyrus kandleri | |
2.8.4.1 | 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 | Methanococcus voltae | |
2.8.4.1 | 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 | Methanoculleus thermophilus | |
2.8.4.1 | 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 | Methanothermobacter marburgensis | |
2.8.4.1 | F-430 | with Ni(I) oxidation state | Methanosarcina barkeri | |
2.8.4.1 | F-430 | with Ni(I) oxidation state | Methanocaldococcus jannaschii | |
2.8.4.1 | F-430 | with Ni(I) oxidation state | Methanococcus voltae | |
2.8.4.1 | F-430 | with Ni(I) oxidation state | Methanoculleus thermophilus | |
2.8.4.1 | F-430 | with Ni(I) oxidation state | Methanothermobacter marburgensis | |
2.8.4.1 | F-430 | with Ni(I) oxidation state | Methanopyrus kandleri |