D
IPR000182

GNAT domain

InterPro entry
Short nameGNAT_dom
Overlapping
homologous
superfamilies
 
domain relationships

Description

The N-acetyltransferases (NAT) (
2.3.1.-
) are enzymes that use acetyl coenzyme A (CoA) to transfer an acetyl group to a substrate, a reaction implicated in various functions from bacterial antibiotic resistance to mammalian circadian rhythm and chromatin remodelling. The Gcn5-related N-acetyltransferases (GNAT) catalyse the transfer of the acetyl from the CoA donor to a primary amine of the acceptor. The GNAT proteins share a domain composed of four conserved sequence motifs A-D
[1, 4]
. This GNAT domain is named after yeast GCN5 (from General Control Nonrepressed) and related histone acetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residues of N-terminal histone tails, resulting in transcription activation. Another category of GNAT, the aminoglycoside N-acetyltransferases, confer antibiotic resistance by catalysing the acetylation of amino groups in aminoglycoside antibiotics
[5]
. GNAT proteins can also have anabolic and catabolic functions in both prokaryotes and eukaryotes
[1, 4, 5, 2, 3]
.

The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to 7 β-strands (B) and 4 helices (H) in the topology B1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may be from the same monomer or contributed by another
[4, 3]
. Motifs D (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core
[4, 2, 3]
, while the N-terminal motif C (B1-H1) is less conserved.

Some proteins known to contain a GNAT domain:


 * Actinobacterial mycothiol acetyltransferase (MshD), which catalyses the transfer of acetyl from acetyl-CoA to desacetylmycothiol to form mycothiol.
 * Yeast GCN5 and Hat1, which are histone acetyltransferases (EC 2.3.1.48).
 * Human PCAF, a histone acetyltransferase.
 * Mammalian serotonin N-acetyltransferase (SNAT) or arylalkylamine NAT (AANAT), which acetylates serotonin into a circadian neurohormone that may participate in light-dark rhythms, and human mood and behaviour.
 * Mammalian glucosamine 6-phosphate N-acetyltransferase (GNA1) (EC 2.3.1.4).
 * Escherichia coli RimI and RimJ, which acetylate the N-terminal alanine of ribosomal proteins S18 and S5, respectively (EC 2.3.1.128).
 * Mycobacterium tuberculosis aminoglycoside 2'-N-acetyltransferase (Aac), which acetylates the 2' hydroxyl or amino group of a broad spectrum of aminoglycoside antibiotics.
 * Bacillus subtilis BltD and PaiA, which acetylate spermine and spermidine.


This entry represents the entire GNAT domain.

References

1.GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Neuwald AF, Landsman D. Trends Biochem. Sci. 22, 154-5, (1997). View articlePMID: 9175471

2.Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation. He H, Ding Y, Bartlam M, Sun F, Le Y, Qin X, Tang H, Zhang R, Joachimiak A, Liu J, Zhao N, Rao Z. J. Mol. Biol. 325, 1019-30, (2003). View articlePMID: 12527305

3.Structure and functions of the GNAT superfamily of acetyltransferases. Vetting MW, S de Carvalho LP, Yu M, Hegde SS, Magnet S, Roderick SL, Blanchard JS. Arch. Biochem. Biophys. 433, 212-26, (2005). View articlePMID: 15581578

4.GCN5-related N-acetyltransferases: a structural overview. Dyda F, Klein DC, Hickman AB. 29, 81-103, (2000). View articlePMID: 10940244

5.X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members. Burk DL, Ghuman N, Wybenga-Groot LE, Berghuis AM. Protein Sci. 12, 426-37, (2003). View articlePMID: 12592013

GO terms

biological process

  • None

cellular component

  • None

Cross References

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