Summary: NAT, N-acetyltransferase, of N-acetylglutamate synthase
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NAT, N-acetyltransferase, of N-acetylglutamate synthase Provide feedback
This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 184.108.40.206. It is also found C-terminal to the amino acid kinase region (PF00696) in some fungal acetylglutamate kinase enzymes . it stabilises the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition by arginine . This domain is found to be the N-acetyltransferase (NAT) domain, and it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25 Angstrom away from the L-arginine binding site in the N-temrinal domain PF00696 .
Shi D, Li Y, Cabrera-Luque J, Jin Z, Yu X, Zhao G, Haskins N, Allewell NM, Tuchman M;, PLoS One. 2011;6:e28825.: A novel N-acetylglutamate synthase architecture revealed by the crystal structure of the bifunctional enzyme from Maricaulis maris. PUBMED:22174908 EPMC:22174908
de Cima S, Gil-Ortiz F, Crabeel M, Fita I, Rubio V;, PLoS One. 2012;7:e34734.: Insight on an arginine synthesis metabolon from the tetrameric structure of yeast acetylglutamate kinase. PUBMED:22529931 EPMC:22529931
Zhao G, Jin Z, Allewell NM, Tuchman M, Shi D;, PLoS One. 2013;8:e70369.: Crystal structure of the N-acetyltransferase domain of human N-acetyl-L-glutamate synthase in complex with N-acetyl-L-glutamate provides insights into its catalytic and regulatory mechanisms. PUBMED:23894642 EPMC:23894642
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR006855
This region of unknown function is found at the C terminus of Neurospora crassa acetylglutamate synthase (EC). It is also found C-terminal to the amino acid kinase region in some fungal acetylglutamate kinase enzymes (INTERPRO). These enzymes play a role in arginine biosynthesis.
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This clan contains families related to N-acetyltransferases. N-acetyltransferases catalyse the transfer of acetyl groups from acetyl-CoA to arylamines.
The clan contains the following 33 members:Acetyltransf_1 Acetyltransf_10 Acetyltransf_13 Acetyltransf_15 Acetyltransf_3 Acetyltransf_4 Acetyltransf_5 Acetyltransf_6 Acetyltransf_7 Acetyltransf_8 Acetyltransf_9 Acetyltransf_CG AstA ATE_C ATE_N Autoind_synth DUF1248 DUF1999 DUF2156 DUF3749 FemAB FemAB_like FR47 Gly_acyl_tr_C GNAT_acetyltr_2 GNAT_acetyltran Leu_Phe_trans Mec-17 Mig-14 MOZ_SAS NAT NMT NodA
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Curation and family details
|Number in seed:||29|
|Number in full:||931|
|Average length of the domain:||163.90 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||27.92 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the NAT domain has been found. There are 57 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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