Summary: Methylaspartate ammonia-lyase C-terminus
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Methylaspartate ammonia-lyase C-terminus Provide feedback
Methylaspartate ammonia-lyase EC:126.96.36.199 catalyses the second step of fermentation of glutamate. It is a homodimer. This family represents the C-terminal region of Methylaspartate ammonia-lyase and contains a TIM barrel fold similar to the PF01188. This family represents the catalytic domain and contains a metal binding site .
Goda SK, Minton NP, Botting NP, Gani D; , Biochemistry 1992;31:10747-10756.: Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein. PUBMED:1420191 EPMC:1420191
Asuncion M, Blankenfeldt W, Barlow JN, Gani D, Naismith JH; , J Biol Chem 2002;277:8306-8311.: The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. PUBMED:11748244 EPMC:11748244
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR022662
Methylaspartate ammonia-lyase EC catalyses the second step of fermentation of glutamate. It is a homodimer. This domain represents the C-terminal region of methylaspartate ammonia-lyase and contains a TIM barrel fold similar to the . This domain represents the catalytic domain and contains a metal binding site [PUBMED:11748244].
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Curation and family details
|Author:||Bateman A, Moxon SJ|
|Number in seed:||14|
|Number in full:||185|
|Average length of the domain:||245.40 aa|
|Average identity of full alignment:||60 %|
|Average coverage of the sequence by the domain:||60.15 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|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 MAAL_C domain has been found. There are 12 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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