Summary: Methylaspartate mutase E chain (MutE)
Methylaspartate mutase E chain (MutE) Provide feedback
This family consists of several methylaspartate mutase E chain proteins ( EC:22.214.171.124). Glutamate mutase catalyses the first step in the fermentation of glutamate by Clostridium tetanomorphum. This is an unusual isomerisation in which L-glutamate is converted to threo-beta-methyl L-aspartate .
Holloway DE, Marsh EN; , J Biol Chem 1994;269:20425-20430.: Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme. PUBMED:8051138 EPMC:8051138
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This tab holds annotation information from the InterPro database.
InterPro entry IPR006396
Glutamate mutase (methylaspartate mutase) catalyses the reversible interconversion of L-glutamate and L-threo-3-methylaspartate, the first step in the pathway of glutamate fermentation [PUBMED:16285720]. Catalysis is initiated using the cobalamin cofactor. The E subunit is the catalytic subunit (MutE) [PUBMED:14738967].
|Molecular function||methylaspartate mutase activity (GO:0050097)|
|Biological process||anaerobic glutamate catabolic process (GO:0019670)|
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Curation and family details
|Seed source:||Pfam-B_14693 (release 9.0)|
|Number in seed:||32|
|Number in full:||104|
|Average length of the domain:||407.10 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||78.59 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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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 Met_asp_mut_E domain has been found. There are 6 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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