Summary: 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
2-oxoacid dehydrogenases acyltransferase (catalytic domain) Provide feedback
These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
Mattevi A, Obmolova G, Kalk KH, Westphal AH, De Kok A, Hol WG; , J Mol Biol 1993;230:1183-1199.: Refined crystal structure of the catalytic domain of dihysrolipoyl transacetylase (E2P) from azotobacter vineelandii at 2.6 angstroms resolution. PUBMED:8487300 EPMC:8487300
Internal database links
|Similarity to PfamA using HHSearch:||CAT|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001078This domain is found in the lipoamide acyltransferase component of the branched-chain alpha-keto acid dehydrogenase complex EC, which catalyses the overall conversion of alpha-keto acids to acyl-CoA and carbon dioxide [PUBMED:8487300]. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The domain is also found in the dihydrolipoamide succinyltransferase component of the 2-oxoglutarate dehydrogenase complex EC. These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||transferase activity, transferring acyl groups (GO:0016746)|
|Biological process||metabolic process (GO:0008152)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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All characterised families in this clan are involved in CoA-dependent acyltransferase. All families have a characteristic HXXXD motif.
The clan contains the following 7 members:2-oxoacid_dh AATase Carn_acyltransf CAT Condensation Transferase WES_acyltransf
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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Curation and family details
|Seed source:||Bateman A|
|Author:||Bateman A, Finn RD, Griffiths-Jones SR|
|Number in seed:||100|
|Number in full:||10039|
|Average length of the domain:||224.80 aa|
|Average identity of full alignment:||35 %|
|Average coverage of the sequence by the domain:||47.20 %|
|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:||18|
|Download:||download the raw HMM for this family|
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There is 1 interaction 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 2-oxoacid_dh domain has been found. There are 65 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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