Summary: Acetyltransferase (GNAT) domain
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Acetyltransferase Edit Wikipedia article
- Histone acetyltransferases including CBP histone acetyltransferase
- Choline acetyltransferase
- Chloramphenicol acetyltransferase
- Serotonin N-acetyltransferase
- NatA Acetyltransferase
- NatB acetyltransferase
|This enzyme-related article is a stub. You can help Wikipedia by expanding it.|
Acetyltransferase (GNAT) domain Provide feedback
This domain catalyses N-acetyltransferase reactions.
Internal database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000182
The N-acetyltransferases (NAT) (EC 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 remodeling. The Gcn5-related N-acetyltransferases (GNAT) catalyze 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 [PUBMED:9175471, PUBMED:10940244]. 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 [PUBMED:12592013]. GNAT proteins can also have anabolic and catabolic functions in both prokaryotes and eukaryotes [PUBMED:9175471, PUBMED:10940244, PUBMED:12592013, PUBMED:12527305, PUBMED:15581578].
The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to 7 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 [PUBMED:10940244, PUBMED:15581578]. Motifs D (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core [PUBMED:10940244, PUBMED:12527305, PUBMED:15581578], 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 126.96.36.199).
- 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 behavior.
- Mammalian glucosamine 6-phosphate N-acetyltransferase (GNA1) (EC 188.8.131.52).
- Escherichia coli rimI and rimJ, which acetylate the N-terminal alanine of ribosomal proteins S18 and S5, respectively (EC 184.108.40.206).
- 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.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||N-acetyltransferase activity (GO:0008080)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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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 39 members:Acetyltransf_1 Acetyltransf_10 Acetyltransf_13 Acetyltransf_15 Acetyltransf_16 Acetyltransf_3 Acetyltransf_4 Acetyltransf_5 Acetyltransf_6 Acetyltransf_7 Acetyltransf_8 Acetyltransf_9 Acetyltransf_CG AstA ATE_C ATE_N Autoind_synth DUF1122 DUF1248 DUF1999 DUF2156 DUF3749 FemAB FemAB_like FR47 Gly_acyl_tr_C GNAT_acetyltr_2 GNAT_acetyltran HAT_KAT11 HlyC Leu_Phe_trans MCD Mig-14 MOZ_SAS NAT NMT NMT_C NodA ODC_AZ
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
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- alignment generated by searching the metagenomics sequence database using the family HMM
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Key: available, not generated, — not available.
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Curation and family details
|Number in seed:||2230|
|Number in full:||6019|
|Average length of the domain:||90.00 aa|
|Average identity of full alignment:||18 %|
|Average coverage of the sequence by the domain:||47.12 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Acetyltransf_7 domain has been found. There are 21 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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