Summary: Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain
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This is the Wikipedia entry entitled "Acetyl-CoA C-myristoyltransferase". More...
Acetyl-CoA C-myristoyltransferase Edit Wikipedia article
In enzymology, an acetyl-CoA C-myristoyltransferase (EC 2.3.1.155) is an enzyme that catalyzes the chemical reaction
- myristoyl-CoA + acetyl-CoA 3-oxopalmitoyl-CoA + CoA
Thus, the two substrates of this enzyme are myristoyl-CoA and acetyl-CoA, whereas its two products are 3-oxopalmitoyl-CoA and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is myristoyl-CoA:acetyl-CoA C-myristoyltransferase.
References
- Miyazawa S, Furuta S, Osumi T, Hashimoto T, Ui N (Tokyo). "Properties of peroxisomal 3-ketoacyl-coA thiolase from rat liver". J. Biochem.: 511–9. PMID 6117552.
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(help)CS1 maint: multiple names: authors list (link)
External links
Gene Ontology (GO) codes
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This is the Wikipedia entry entitled "Glycylpeptide N-tetradecanoyltransferase". More...
Glycylpeptide N-tetradecanoyltransferase Edit Wikipedia article
In enzymology, a glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) is an enzyme that catalyzes the chemical reaction
- tetradecanoyl-CoA + glycylpeptide CoA + N-tetradecanoylglycylpeptide
Thus, the two substrates of this enzyme are tetradecanoyl-CoA and glycylpeptide, whereas its two products are CoA and N-tetradecanoylglycylpeptide.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is tetradecanoyl-CoA:glycylpeptide N-tetradecanoyltransferase. Other names in common use include peptide N-myristoyltransferase, myristoyl-CoA-protein N-myristoyltransferase, myristoyl-coenzyme A:protein N-myristoyl transferase, myristoylating enzymes, and protein N-myristoyltransferase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1IIC, 1IID, 1IYK, 1IYL, 1RXT, 2NMT, 2P6E, 2P6F, and 2P6G.
References
- Guertin D, Grise-Miron L, Riendeau D (1986). "Identification of a 51-kilodalton polypeptide fatty acyl chain acceptor in soluble extracts from mouse cardiac tissue". Biochem. Cell. Biol. 64: 1249–55. PMID 3566958.
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: CS1 maint: multiple names: authors list (link) - Heuckeroth RO, Towler DA, Adams SP, Glaser L, Gordon JI (1988). "11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase". J. Biol. Chem. 263: 2127–33. PMID 3123489.
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: CS1 maint: multiple names: authors list (link)
External links
- The CAS registry number for this enzyme class is Template:CAS registry.
Gene Ontology (GO) codes
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
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.
Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain Provide feedback
The N and C-terminal domains of NMT are structurally similar, each adopting an acyl-CoA N-acyltransferase-like fold.
Literature references
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Weston SA, Camble R, Colls J, Rosenbrock G, Taylor I, Egerton M, Tucker AD, Tunnicliffe A, Mistry A, Mancia F, de la Fortelle E, Irwin J, Bricogne G, Pauptit RA; , Nat Struct Biol 1998;5:213-221.: Crystal structure of the anti-fungal target N-myristoyl transferase. PUBMED:9501915 EPMC:9501915
External database links
PROSITE: | PDOC00752 |
SCOP: | 2nmt |
This tab holds annotation information from the InterPro database.
InterPro entry IPR022677
Myristoyl-CoA:protein N-myristoyltransferase ( EC ) (Nmt) [ PUBMED:8322618 ] is the enzyme responsible for transferring a myristate group on the N-terminal glycine of a number of cellular eukaryotics and viral proteins. Nmt is a monomeric protein of about 50 to 60kDa whose sequence appears to be well conserved.
The N and C-terminal domains of NMT are structurally similar, each adopting an acyl-CoA N-acyltransferase-like fold. This entry represents the C-terminal region.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | glycylpeptide N-tetradecanoyltransferase activity (GO:0004379) |
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 Acetyltrans (CL0257), which has the following description:
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 50 members:
Acetyltransf_1 Acetyltransf_10 Acetyltransf_13 Acetyltransf_15 Acetyltransf_16 Acetyltransf_17 Acetyltransf_18 Acetyltransf_19 Acetyltransf_3 Acetyltransf_4 Acetyltransf_5 Acetyltransf_6 Acetyltransf_7 Acetyltransf_8 Acetyltransf_9 Acetyltransf_CG AstA ATE_C ATE_N Autoind_synth CFAP61_N DUF1122 DUF1248 DUF1999 DUF5613 DUF5645 FemAB FemAB_like FR47 Gly_acyl_tr_C GNAT_acetyltr_2 GNAT_acetyltran GNAT_C GNAT_like HAT_KAT11 HlyC Leu_Phe_trans LPG_synthase_C MCD Mig-14 MOZ_SAS NAT NMT NMT_C NodA ODC_AZ PanZ Phage_T7_Gp13 Pho86 T_hemolysinAlignments
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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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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 (148) |
Full (2656) |
Representative proteomes | UniProt (4517) |
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RP15 (505) |
RP35 (1164) |
RP55 (2068) |
RP75 (2752) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (148) |
Full (2656) |
Representative proteomes | UniProt (4517) |
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RP15 (505) |
RP35 (1164) |
RP55 (2068) |
RP75 (2752) |
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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.
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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.
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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: | Prosite |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Finn RD |
Number in seed: | 148 |
Number in full: | 2656 |
Average length of the domain: | 187.2 aa |
Average identity of full alignment: | 49 % |
Average coverage of the sequence by the domain: | 39.34 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 212 | ||||||||||||
Family (HMM) version: | 18 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
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 NMT_C domain has been found. There are 243 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 sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.