InterPro : IPR000182

Name  GNAT domain Short Name  GNAT_dom
Type  Domain 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 is named after yeast GCN5 (from General Control Nonrepressed) and related histone acetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residues of amino terminal histone tails, resulting in transcription activation. Another category of GNAT, the aminoglycoside N-acetyltransferases, confer antibiotic resistance by catalyzing the acetylation of amino groups in aminoglycoside antibiotics []. GNAT proteins can also have anabolic and catabolic 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 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 [, ]. Motifs D (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.Some proteins known to contain a GNAT domain: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 mayparticipate in light-dark rhythms, and human mood and behavior.Mammalian glucosamine 6-phosphate N-acetyltransferase (GNA1) (EC 2.3.1.4).Escherichia coli rimI and rimJ, which acetylate the N-terminal alanine ofribosomal 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 ofaminoglycoside antibiotics.Bacillus subtilis bltD and paiA, which acetylate spermine and spermidine.This entry represents the entire GNAT domain.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

14 Found In

Id Name Short Name Type
IPR005910 Histone acetyltransferase ELP3 Hist_AcTrfase_ELP3 Family
IPR016376 Histone acetylase PCAF Hist_acetylase_PCAF Family
IPR012752 TDP-D-fucosamine acetyltransferase WecD AcTrfase_WecD Family
IPR016794 Uncharacterised conserved protein UCP21603, acetyltransferase-like UCP21603_acetyltransf Family
IPR005216 Citrate lyase ligase Citrate_lyase_ligase Family
IPR016890 Uncharacterised conserved protein UCP028520 UCP028520 Family
IPR017255 Acetyltransferase, GNAT, predicted AcTrfase_GNAT_prd Family
IPR017274 Putative N-acetyltransferase YlbP YlbP Family
IPR017534 GNAT-acetyltransferase GNAT-acetyltransferase Family
IPR017813 Mycothiol acetyltransferase Mycothiol_AcTrfase Family
IPR008125 Streptothricin acetyltransferase Streptothricin_AcTrfase Family
IPR010167 Amino-acid N-acetyltransferase (ArgA) NH2A_AcTrfase_ArgA Family
IPR011244 Bifunctional argininosuccinate lyase/acetyltransferase ASAL_AGS_AcTrfase Family
IPR012772 L-2,4-diaminobutyric acid acetyltransferase Ectoine_EctA Family

1 Parent Features

Id Name Short Name Type
IPR016181 Acyl-CoA N-acyltransferase Acyl_CoA_acyltransferase Domain

5 Publications

First Author Title Year Journal Volume Pages
Neuwald AF GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. 1997 Trends Biochem Sci 22 154-5
He H Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation. 2003 J Mol Biol 325 1019-30
Burk DL X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members. 2003 Protein Sci 12 426-37
Dyda F GCN5-related N-acetyltransferases: a structural overview. 2000 Annu Rev Biophys Biomol Struct 29 81-103
Vetting MW Structure and functions of the GNAT superfamily of acetyltransferases. 2005 Arch Biochem Biophys 433 212-26



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)