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243  structures 1530  species 0  interactions 2656  sequences 66  architectures

Family: NMT_C (PF02799)

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

acetyl-CoA C-myristoyltransferase
EC number2.3.1.155
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain

In enzymology, an acetyl-CoA C-myristoyltransferase (EC 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.


  • Miyazawa S, Furuta S, Osumi T, Hashimoto T, Ui N (August 1981). "Properties of peroxisomal 3-ketoacyl-coA thiolase from rat liver". J. Biochem. Tokyo. 90 (2): 511–9. PMID 6117552.

External links

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

  1. 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

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.

Domain organisation

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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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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...


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

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Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD , Bateman A , Griffiths-Jones SR
Number in seed: 148
Number in full: 2656
Average length of the domain: 187.20 aa
Average identity of full alignment: 49 %
Average coverage of the sequence by the domain: 39.34 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.9 27.9
Trusted cut-off 28.0 28.4
Noise cut-off 26.5 26.7
Model length: 212
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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 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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