| Primary Identifier | IPR006855 | Type | Domain |
| Short Name | Vertebrate-like_GNAT_dom |
| description | The N-acetyltransferases (NAT) (EC 2.3.1.-) are enzymes that use acetylcoenzyme A (CoA) to transfer an acetyl group to a substrate, a reactionimplicated in various functions from bacterial antibiotic resistance tomammalian circadian rhythm and chromatin remodeling. The Gcn5-relatedN-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the CoAdonor to a primary amine of the acceptor. The GNAT proteins share a domaincomposed of four conserved sequence motifs A-D [, ]. This GNAT domain isnamed after yeast GCN5 (from General Control Nonrepressed) and related histoneacetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residuesof amino terminal histone tails, resulting in transcription activation.Another category of GNAT, the aminoglycoside N-acetyltransferases, conferantibiotic resistance by catalyzing the acetylation of amino groups inaminoglycoside antibiotics []. GNAT proteins can also have anabolic andcatabolic functions in both prokaryotes and eukaryotes [, , , , ].The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to7 beta strands (B) and 4 helices (H) in the topologyB1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may befrom the same monomer or contributed by another [, ]. MotifsD (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core[, , ], while the N-terminal motif C (B1-H1) is less conserved.This entry represents the vertebrate-likeNAGS-type GNAT domain []. |
