14  structures 39  species 4  interactions 51  sequences 1  architecture

Family: MCR_gamma (PF02240)

Summary

Methyl-coenzyme M reductase gamma subunit Add an annotation

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 (PF02241), and 2 gamma (this family) subunits with two identical nickel porphinoid active sites [1].


Literature references

  1. 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


InterPro entry IPR003178

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 (), 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 gamma subunit, which has a complex alpha-helical/beta-sheet topology.

Gene Ontology

External database links

Domain organisation

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Alignments

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The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

Pfam alignments:
Full length sequences

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MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.

Pfam alignments:

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Trees

This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.

Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_2713 (release 5.2)
Previous IDs: none
Type: Domain
Author: Mian N, Bateman A
Number in seed: 7
Number in full: 51
Average length of the domain: 247.10 aa
Average identity of full alignment: 59 %
Average coverage of the sequence by the domain: 93.62 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 339.0 339.0
Noise cut-off 18.6 18.0
Model length: 247
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 4 interactions for this family. More...

MCR_beta MCR_alpha_N MCR_alpha MCR_beta_N

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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_gamma domain has been found.

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