SMART: Pfam domain Bile_Hydr

The domain within your query sequence starts at position 15 and ends at position 144; the E-value for the Bile_Hydr_Trans domain shown below is 6e-44.

DEPVSIRATGLPPSQIVTIKATVKDENDNVFQSQAFYKTNEAGEVDLEKTPALGGDYVGV
HPMGLFFSLKPKKAFHRLMKKDVMNSPLCICLDLYDSVNWLETVRIPSKASQRVQRWFVG
PGVKREQIQE

Bile_Hydr_Trans

PFAM accession number:	PF04775
Interpro abstract (IPR006862):	This entry presents the N-termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT) [ (PUBMED:11673457) ]. This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism [ (PUBMED:10567408) ]. For example, in peroxisomes, the hydrolase acts on bile-CoA esters [ (PUBMED:11673457) ].

PFAM accession number:

PF04775

Interpro abstract (IPR006862):

This entry presents the N-termini of acyl-CoA thioester hydrolase and bile acid-CoA:amino acid N-acetyltransferase (BAAT) [ (PUBMED:11673457) ]. This region is not thought to contain the active site of either enzyme. Thioesterase isoforms have been identified in peroxisomes, cytoplasm and mitochondria, where they are thought to have distinct functions in lipid metabolism [ (PUBMED:10567408) ]. For example, in peroxisomes, the hydrolase acts on bile-CoA esters [ (PUBMED:11673457) ].

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