Summary: LeuA allosteric (dimerisation) domain
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LeuA allosteric (dimerisation) domain Provide feedback
This is the C-terminal regulatory (R) domain of alpha-isopropylmalate synthase, which catalyses the first committed step in the leucine biosynthetic pathway . This domain, is an internally duplicated structure with a novel fold . It comprises two similar units that are arranged such that the two -helices pack together in the centre, crossing at an angle of 34 degrees, sandwiched between the two three-stranded, antiparallel beta-sheets. The overall domain is thus constructed as a beta-alpha-beta three-layer sandwich .
Koon N, Squire CJ, Baker EN; , Proc Natl Acad Sci U S A 2004;101:8295-8300.: Crystal structure of LeuA from Mycobacterium tuberculosis, a key enzyme in leucine biosynthesis. PUBMED:15159544 EPMC:15159544
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013709
This is the C-terminal regulatory (R) domain of alpha-isopropylmalate synthase, which catalyses the first committed step in the leucine biosynthetic pathway [PUBMED:15159544]. This domain, is an internally duplicated structure with a novel fold [PUBMED:15159544]. It comprises two similar units that are arranged such that the two -helices pack together in the centre, crossing at an angle of 34 degrees, sandwiched between the two three-stranded, antiparallel beta-sheets. The overall domain is thus constructed as a beta-alpha-beta three-layer sandwich [PUBMED:15159544].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||2-isopropylmalate synthase activity (GO:0003852)|
|Biological process||leucine biosynthetic process (GO:0009098)|
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Curation and family details
|Seed source:||Pfam-B_223 (release 18.0)|
|Number in seed:||53|
|Number in full:||19711|
|Average length of the domain:||134.40 aa|
|Average identity of full alignment:||30 %|
|Average coverage of the sequence by the domain:||25.62 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
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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 LeuA_dimer domain has been found. There are 14 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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