SMART: Pfam domain BPL_LplA

The domain within your query sequence starts at position 74 and ends at position 185; the E-value for the BPL_LplA_LipB domain shown below is 4.5e-24.

IGRHQNPWQECNLHLMRQEGIKLARRKSGGGAVYHDMGNINLTFFTTKTKYDRMENLKLI
VRALNAVQPQLDVQPTKKFDLLLDGQFKISGTASKIGRTAAYHHCTLLCSTN

BPL_LplA_LipB

PFAM accession number:	PF03099
Interpro abstract (IPR004143):	Biotin and lipoic acid are the covalently bound cofactors of various multicomponent enzyme complexes that catalyze key metabolic reactions. In these enzymes complexes, biotin and lipoic acid are attached via amide linkage through their carboxyl group and the epsilon-amino group of a specific lysine residue of a protein module known respectively as the biotinyl and the lipoyl domain. Covalent attachment of biotin and lipoic acid to these enzyme complexes occurs post-translationally, and it is mediated by biotinylating and lipoylating protein enzymes, which specifically recognise the biotinyl and lipoyl domains, ensuring their correct post-translational modification. Lipoylating and biotinylating enzymes are evolutionarily related protein families containing a homologous catalytic module [ (PUBMED:11106165) ]. Amino acid sequence conservation between the catalytic modules of biotinyl protein ligases (BPLs) and lipoyl protein ligases (LPLs) is very low, and mainly affects residues that are important for the scaffold of the structure, such as those contributing to the hydrophobic core. Despite the poor overall sequence similarity, a single lysine residue is strictly conserved in all LPL and BPL sequences. This lysine residue is likely to bind specifically to the carbonyl oxygen of the carboxyl group of biotin or at the end of the hydrogen- carbon tail of the lipoyl moiety [ (PUBMED:11106165) ]. The BPL/LPL catalytic domain contains a seven-stranded mixed beta-sheet on one side and four alpha-helices on the other side [ (PUBMED:16169557) ].
GO process:	cellular protein modification process (GO:0006464)

PFAM accession number:

PF03099

Interpro abstract (IPR004143):

Biotin and lipoic acid are the covalently bound cofactors of various multicomponent enzyme complexes that catalyze key metabolic reactions. In these enzymes complexes, biotin and lipoic acid are attached via amide linkage through their carboxyl group and the epsilon-amino group of a specific lysine residue of a protein module known respectively as the biotinyl and the lipoyl domain. Covalent attachment of biotin and lipoic acid to these enzyme complexes occurs post-translationally, and it is mediated by biotinylating and lipoylating protein enzymes, which specifically recognise the biotinyl and lipoyl domains, ensuring their correct post-translational modification. Lipoylating and biotinylating enzymes are evolutionarily related protein families containing a homologous catalytic module [ (PUBMED:11106165) ].

Amino acid sequence conservation between the catalytic modules of biotinyl protein ligases (BPLs) and lipoyl protein ligases (LPLs) is very low, and mainly affects residues that are important for the scaffold of the structure, such as those contributing to the hydrophobic core. Despite the poor overall sequence similarity, a single lysine residue is strictly conserved in all LPL and BPL sequences. This lysine residue is likely to bind specifically to the carbonyl oxygen of the carboxyl group of biotin or at the end of the hydrogen- carbon tail of the lipoyl moiety [ (PUBMED:11106165) ]. The BPL/LPL catalytic domain contains a seven-stranded mixed beta-sheet on one side and four alpha-helices on the other side [ (PUBMED:16169557) ].

GO process:

cellular protein modification process (GO:0006464)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry BPL_LplA_LipB