GNAT domain
Short name | GNAT_dom |
Overlapping homologous superfamilies | |
domain relationships |
Description
* 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.
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
molecular function
cellular component
- None
Cross References
PROSITE Doc
ENZYME
- 2.3.1.-
- 2.3.1.1
- 2.3.1.110
- 2.3.1.17
- 2.3.1.178
- 2.3.1.183
- 2.3.1.189
- 2.3.1.193
- 2.3.1.202
- 2.3.1.210
- 2.3.1.228
- 2.3.1.254
- 2.3.1.255
- 2.3.1.256
- 2.3.1.257
- 2.3.1.258
- 2.3.1.259
- 2.3.1.264
- 2.3.1.266
- 2.3.1.267
- 2.3.1.271
- 2.3.1.280
- 2.3.1.308
- 2.3.1.311
- 2.3.1.33
- 2.3.1.36
- 2.3.1.4
- 2.3.1.48
- 2.3.1.53
- 2.3.1.57
- 2.3.1.59
- 2.3.1.60
- 2.3.1.80
- 2.3.1.82
- 2.3.1.87
- 2.3.2.-
- 2.7.1.190
- 2.7.11.1
- 2.7.2.8
- 2.8.1.-
- 4.3.2.1
- 6.2.1.22
- 6.3.5.2
Genome Properties