Summary: N-acetyltransferase
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This is the Wikipedia entry entitled "Acetyltransferase". More...
Acetyltransferase Edit Wikipedia article
Acetyltransferase (or transacetylase) is a type of transferase enzyme that transfers an acetyl group.
Examples include:
- Histone acetyltransferases including CBP histone acetyltransferase
- Choline acetyltransferase
- Chloramphenicol acetyltransferase
- Serotonin N-acetyltransferase
- NatA Acetyltransferase
- NatB acetyltransferase
[edit] See also
[edit] External links
- Acetyltransferases at the US National Library of Medicine Medical Subject Headings (MeSH)
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
N-acetyltransferase Provide feedback
Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of approximately 30kDa. It facilitates the transfer of an acetyl group from Acetyl Coenzyme A on to a wide range of arylamine, N-hydroxyarylamines and hydrazines. Acetylation of these compounds generally results in inactivation. NAT is found in many species from Mycobacteria (M. tuberculosis, M. smegmatis etc) to man. It was the first enzyme to be observed to have polymorphic activity amongst human individuals. NAT is responsible for the inactivation of Isoniazid (a drug used to treat Tuberculosis) in humans. The NAT protein has also been shown to be involved in the breakdown of folic acid.
External database links
| PANDIT: | PF00797 |
| Pseudofam: | PF00797 |
| SCOP: | 1e2t |
| SYSTERS: | Acetyltransf_2 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR001447
Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of approximately 30 kDa. It facilitates the transfer of an acetyl group from acetyl coenzyme A on to a wide range of arylamine, N-hydroxyarylamines and hydrazines. Acetylation of these compounds generally results in inactivation. NAT is found in many species from Mycobacteria (Mycobacterium tuberculosis, Mycobacterium smegmatis etc) to Homo sapiens (Human). It was the first enzyme to be observed to have polymorphic activity amongst human individuals. NAT is responsible for the inactivation of Isoniazid (a drug used to treat tuberculosis) in humans. The NAT protein has also been shown to be involved in the breakdown of folic acid. NAT catalyses the reaction:
NAT is the target of a common genetic polymorphism of clinical relevance in humans. The N-acetylation polymorphism is determined by low or high NAT activity in liver. NAT has been implicated in the action and toxicity of amine-containing drugs, and in the susceptibility to cancer and systematic lupus erythematosus. Two highly similar human genes for NAT, termed NAT1 and NAT2, encode genetically invariant and variant NAT proteins, respectively.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | acetyltransferase activity (GO:0016407) |
| Biological process | metabolic process (GO:0008152) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Peptidase_CA (CL0125), which contains the following 60 members:
Acetyltransf_2 Amidase_5 Amidase_6 CHAP DUF1175 DUF1287 DUF1460 DUF2272 DUF3335 DUF553 DUF830 EDR1 Guanylate_cyc_2 LRAT NLPC_P60 OTU Peptidase_C1 Peptidase_C10 Peptidase_C12 Peptidase_C16 Peptidase_C1_2 Peptidase_C2 Peptidase_C21 Peptidase_C23 Peptidase_C27 Peptidase_C28 Peptidase_C31 Peptidase_C32 Peptidase_C33 Peptidase_C34 Peptidase_C36 Peptidase_C39 Peptidase_C39_2 Peptidase_C42 Peptidase_C47 Peptidase_C48 Peptidase_C5 Peptidase_C54 Peptidase_C58 Peptidase_C6 Peptidase_C65 Peptidase_C7 Peptidase_C70 Peptidase_C71 Peptidase_C78 Peptidase_C8 Peptidase_C9 Peptidase_C93 Peptidase_C98 Phytochelatin Rad4 Transglut_core Transglut_core2 Transglut_core3 Transglut_i_TM Transpep_BrtH UCH UCH_1 Viral_protease YopJAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (33) |
Full (2001) |
Representative proteomes | NCBI (1384) |
Meta (26) |
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| RP15 (133) |
RP35 (234) |
RP55 (337) |
RP75 (435) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
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Format an alignment
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (33) |
Full (2001) |
Representative proteomes | NCBI (1384) |
Meta (26) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (133) |
RP35 (234) |
RP55 (337) |
RP75 (435) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_575 (release 2.1) |
| Previous IDs: | Acetyltransf2; |
| Type: | Family |
| Author: | Bateman A |
| Number in seed: | 33 |
| Number in full: | 2001 |
| Average length of the domain: | 229.20 aa |
| Average identity of full alignment: | 28 % |
| Average coverage of the sequence by the domain: | 85.40 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 240 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
Acetyltransf_2Structures
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_2 domain has been found. There are 31 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence