SMART: Pfam domain Acetyltransf

The domain within your query sequence starts at position 20 and ends at position 280; the E-value for the Acetyltransf_2 domain shown below is 3.3e-98.

DLKTLTEILQHQIRAIPFENLNIHCGESMELSLEAIFDQIVRKKRGGWCLQVNHLLYWAL
TKLGFETTMLGGYVFNTPANKYSSGMIHLLVQVTISGKDYIVDAGFGRSYQMWEPLELTS
GKDQPQVPAIFRLTEENGTWYLDQIRREQYVPNQEFINSDLLEKNKYRKIYSFTLEPRTI
EDFESMNTYLQTSPASVFTSKSFCSLQTPEGVHCLVGSTLTYRRFSYKDNVDLVEFKSLT
EEEIEDVLRTIFGVSLERKLV

Acetyltransf_2

PFAM accession number:	PF00797
Interpro abstract (IPR001447):	Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of approximately 30kDa. It facilitates the transfer of an acetyl group from acetyl coenzyme A on to a wide range of arylamine, N-hydroxyarylamines and hydrazines. Acetylation of these compounds generally results in inactivation. NAT is found in many species from Mycobacteria (Mycobacterium tuberculosis, Mycobacterium smegmatis etc) to Homo sapiens (Human). It was the first enzyme to be observed to have polymorphic activity amongst human individuals. NAT is responsible for the inactivation of Isoniazid (a drug used to treat tuberculosis) in humans. The NAT protein has also been shown to be involved in the breakdown of folic acid. NAT catalyses the reaction: Acetyl-coA + arylamine = coA + N-acetylarylamine NAT is the target of a common genetic polymorphism of clinical relevance in humans. The N-acetylation polymorphism is determined by low or high NAT activity in liver. NAT has been implicated in the action and toxicity of amine-containing drugs, and in the susceptibility to cancer and systematic lupus erythematosus. Two highly similar human genes for NAT, termed NAT1 and NAT2, encode genetically invariant and variant NAT proteins, respectively.
GO function:	acetyltransferase activity (GO:0016407)

PFAM accession number:

PF00797

Interpro abstract (IPR001447):

Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of approximately 30kDa. It facilitates the transfer of an acetyl group from acetyl coenzyme A on to a wide range of arylamine, N-hydroxyarylamines and hydrazines. Acetylation of these compounds generally results in inactivation. NAT is found in many species from Mycobacteria (Mycobacterium tuberculosis, Mycobacterium smegmatis etc) to Homo sapiens (Human). It was the first enzyme to be observed to have polymorphic activity amongst human individuals. NAT is responsible for the inactivation of Isoniazid (a drug used to treat tuberculosis) in humans. The NAT protein has also been shown to be involved in the breakdown of folic acid. NAT catalyses the reaction:

Acetyl-coA + arylamine = coA + N-acetylarylamine

NAT is the target of a common genetic polymorphism of clinical relevance in humans. The N-acetylation polymorphism is determined by low or high NAT activity in liver. NAT has been implicated in the action and toxicity of amine-containing drugs, and in the susceptibility to cancer and systematic lupus erythematosus. Two highly similar human genes for NAT, termed NAT1 and NAT2, encode genetically invariant and variant NAT proteins, respectively.

GO function:

acetyltransferase activity (GO:0016407)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Acetyltransf_2