Summary: Mandelate racemase / muconate lactonizing enzyme, C-terminal domain
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Mandelate racemase / muconate lactonizing enzyme, C-terminal domain Provide feedback
C-terminal domain is TIM barrel fold, dehydratase-like domain. Manganese is associated with this domain.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013342
Mandelate racemase EC (MR) and muconate lactonising enzyme EC (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyse mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures [PUBMED:2215699, PUBMED:8256284]. A number of other proteins also seem to be evolutionary related to these two enzymes. These include, various plasmid-encoded chloromuconate cycloisomerases EC, Escherichia coli protein rspA [PUBMED:7545940], E. coli bifunctional DGOA protein, E. coli hypothetical proteins ycjG, yfaW and yidU and a hypothetical protein from Streptomyces ambofaciens [PUBMED:8277241].
This entry represents the C-terminal region of these proteins.
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Curation and family details
|Author:||Finn RD, Bateman A, Griffiths-Jones SR|
|Number in seed:||1272|
|Number in full:||5681|
|Average length of the domain:||69.00 aa|
|Average identity of full alignment:||28 %|
|Average coverage of the sequence by the domain:||18.12 %|
|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:||16|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 MR_MLE domain has been found. There are 582 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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