Summary: Methyl-coenzyme M reductase beta subunit, C-terminal domain
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Methyl-coenzyme M reductase beta subunit, C-terminal domain Provide feedback
Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (PF02249), 2 beta (this family), and 2 gamma (PF02240) subunits with two identical nickel porphinoid active sites . The C-terminal domain of MCR beta has an all-alpha fold with buried central helix.
Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK; , Science 1997;278:1457-1462.: Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation PUBMED:9367957 EPMC:9367957
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This tab holds annotation information from the InterPro database.
InterPro entry IPR022679
Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to methane and the corresponding heterosulphide CoM-S-S-CoB (EC), the final step in methane biosynthesis. This reaction proceeds under anaerobic conditions by methanogenic Archaea [PUBMED:16260307], and requires a nickel-porphinoid prosthetic group, coenzyme F430, which is in the EPR-detectable Ni(I) oxidation state in the active enzyme. Studies on a catalytically inactive enzyme aerobically co-crystallized with coenzyme M displayed a fully occupied coenzyme M-binding site with no alternate conformations. The binding of coenzyme M appears to induce specific conformational changes that suggests a molecular mechanism by which the enzyme ensures that methyl-coenzyme M enters the substrate channel prior to coenzyme B, as required by the active-site geometry [PUBMED:11491299].
MCR is a hexamer composed of 2 alpha, 2 beta, and 2 gamma subunits with two identical nickel porphinoid active sites, which form two long active site channels with F430 embedded at the bottom [PUBMED:9367957, PUBMED:16234924].
This entry represents the C-terminal domain from the beta subunit of methyl-conenzyme M reductase (MCR). The C-terminal domain of MCR beta has an all-alpha fold with buried central helix. This entry is found in assocation with .
|Molecular function||coenzyme-B sulfoethylthiotransferase activity (GO:0050524)|
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Curation and family details
|Seed source:||Pfam-B_2692 (release 5.2)|
|Author:||Mian N, Bateman A, Griffiths-Jones SR|
|Number in seed:||6|
|Number in full:||82|
|Average length of the domain:||252.00 aa|
|Average identity of full alignment:||65 %|
|Average coverage of the sequence by the domain:||57.60 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the MCR_beta domain has been found. There are 31 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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