UniProt functional annotation for P11562



	UniProt functional annotation for P11562

UniProt code: P11562.

Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum).

Taxonomy: Archaea; Euryarchaeota; Methanomada group; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanothermobacter.

Function: Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis (PubMed:2269306, PubMed:3350018). Neither N-6-mercaptohexanoylthreonine phosphate (H-S-HxoTP) nor N-8-mercaptooctanoylthreonine phosphate (H- SOcoTP) nor any other thiol compound such as CoA or CoM can substitute for CoB as the electron donor (PubMed:3350018). {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:3350018}.

Catalytic activity: Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methane; Xref=Rhea:RHEA:12532, ChEBI:CHEBI:16183, ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=2.8.4.1; Evidence={ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:25691570, ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533; Evidence={ECO:0000269|PubMed:27140643, ECO:0000305|PubMed:3350018};

Cofactor: Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; Evidence={ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728, ECO:0000269|PubMed:9367957}; Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state (PubMed:9030728). {ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9030728, ECO:0000269|PubMed:9367957};

Activity regulation: Methyl-coenzyme M reductase activity is inhibited by 3-nitrooxypropanol (3-NOP) in vitro and in vivo, by oxidation of its active site Ni(I), which stops both growth and methanogenesis (PubMed:27140643). Is also inhibited by the reaction product CoM-S-S- CoB (PubMed:3350018). {ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}.

Pathway: One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1. {ECO:0000269|PubMed:27140643, ECO:0000269|PubMed:3350018}.

Subunit: MCR is a hexamer of two alpha, two beta, and two gamma chains, forming a dimer of heterotrimers. {ECO:0000269|PubMed:2269306, ECO:0000269|PubMed:3350018, ECO:0000269|PubMed:9367957}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:23533332}. Note=Under growth limiting conditions on nickel-depleted media, a fraction of 70% of the enzyme is localized close to the cytoplasmic membrane, which implies 'facultative' membrane association of the enzyme. {ECO:0000269|PubMed:23533332}.

Developmental stage: There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contain mostly MCR I. {ECO:0000269|PubMed:2269306}.

Miscellaneous: The MCR reaction has been shown to follow an ordered bi- bi ternary complex mechanism, in which methyl-SCoM must enter the MCR active site prior to CoB for a productive catalysis. {ECO:0000269|PubMed:25691570}.

Similarity: Belongs to the methyl-coenzyme M reductase gamma subunit family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum).
Taxonomy:		Archaea; Euryarchaeota; Methanomada group; Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanothermobacter.



Function:		Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis (PubMed:2269306, PubMed:3350018). Neither N-6-mercaptohexanoylthreonine phosphate (H-S-HxoTP) nor N-8-mercaptooctanoylthreonine phosphate (H- SOcoTP) nor any other thiol compound such as CoA or CoM can substitute for CoB as the electron donor (PubMed:3350018). {ECO:0000269\|PubMed:2269306, ECO:0000269\|PubMed:3350018}.


Catalytic activity:		Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methane; Xref=Rhea:RHEA:12532, ChEBI:CHEBI:16183, ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=2.8.4.1; Evidence={ECO:0000269\|PubMed:2269306, ECO:0000269\|PubMed:25691570, ECO:0000269\|PubMed:27140643, ECO:0000269\|PubMed:3350018}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12533; Evidence={ECO:0000269\|PubMed:27140643, ECO:0000305\|PubMed:3350018};
Cofactor:		Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; Evidence={ECO:0000269\|PubMed:3350018, ECO:0000269\|PubMed:9030728, ECO:0000269\|PubMed:9367957}; Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state (PubMed:9030728). {ECO:0000269\|PubMed:3350018, ECO:0000269\|PubMed:9030728, ECO:0000269\|PubMed:9367957};
Activity regulation:		Methyl-coenzyme M reductase activity is inhibited by 3-nitrooxypropanol (3-NOP) in vitro and in vivo, by oxidation of its active site Ni(I), which stops both growth and methanogenesis (PubMed:27140643). Is also inhibited by the reaction product CoM-S-S- CoB (PubMed:3350018). {ECO:0000269\|PubMed:27140643, ECO:0000269\|PubMed:3350018}.
Pathway:		One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1. {ECO:0000269\|PubMed:27140643, ECO:0000269\|PubMed:3350018}.
Subunit:		MCR is a hexamer of two alpha, two beta, and two gamma chains, forming a dimer of heterotrimers. {ECO:0000269\|PubMed:2269306, ECO:0000269\|PubMed:3350018, ECO:0000269\|PubMed:9367957}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:23533332}. Note=Under growth limiting conditions on nickel-depleted media, a fraction of 70% of the enzyme is localized close to the cytoplasmic membrane, which implies 'facultative' membrane association of the enzyme. {ECO:0000269\|PubMed:23533332}.
Developmental stage:		There are two MCR complexes in this bacteria. MCR II is expressed in the early growth phase. Late growth cells contain mostly MCR I. {ECO:0000269\|PubMed:2269306}.
Miscellaneous:		The MCR reaction has been shown to follow an ordered bi- bi ternary complex mechanism, in which methyl-SCoM must enter the MCR active site prior to CoB for a productive catalysis. {ECO:0000269\|PubMed:25691570}.
Similarity:		Belongs to the methyl-coenzyme M reductase gamma subunit family. {ECO:0000305}.