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Identification
NameGlycylpeptide N-tetradecanoyltransferase
Synonyms
  • Cell division control protein 72
  • Myristoyl-CoA:protein N-myristoyltransferase
  • NMT
  • Peptide N-myristoyltransferase
Gene NameNMT1
Enzyme Class
Biological Properties
General FunctionInvolved in glycylpeptide N-tetradecanoyltransferase activity
Specific FunctionAdds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N- terminal glycine in the nascent polypeptide substrates. Uncharged amino acids are preferred at position 2 while neutral residues are favored at positions 3 and 4. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6
Cellular LocationCytoplasm
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
glycylpeptide + Tetradecanoyl-CoA hydron + Coenzyme A + N-tetradecanoylglycylpeptide
Metabolites
YMDB IDNameView
YMDB00045Coenzyme AShow
YMDB00099Tetradecanoyl-CoA Show
YMDB00528myristoyl-CoAShow
YMDB00862hydronShow
GO Classification
Component
Not Available
Function
glycylpeptide N-tetradecanoyltransferase activity
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
acyltransferase activity
N-acyltransferase activity
Process
protein amino acid lipidation
N-terminal protein lipidation
N-terminal protein myristoylation
metabolic process
macromolecule metabolic process
macromolecule modification
protein modification process
Gene Properties
Chromosome Locationchromosome 12
LocusYLR195C
Gene Sequence>1368 bp ATGTCAGAAGAGGATAAAGCGAAAAAATTAGAGAATTTATTGAAGTTATTACAGTTGAAT AATGACGATACTTCAAAATTCACTCAAGAACAGAAAAAAGCTATGAAAGACCACAAATTC TGGAGAACGCAACCGGTCAAAGATTTCGATGAAAAGGTGGTGGAAGAAGGCCCCATTGAT AAGCCAAAGACACCGGAAGATATATCTGACAAGCCACTACCTTTATTGTCTAGCTTCGAA TGGTGTAGTATTGATGTGGACAACAAAAAACAGCTTGAAGATGTTTTCGTTCTACTAAAT GAAAACTACGTGGAAGACCGCGATGCAGGCTTCAGATTTAACTATACCAAAGAATTCTTC AATTGGGCTTTAAAGAGTCCAGGTTGGAAGAAGGATTGGCATATTGGTGTTCGCGTTAAA GAAACACAGAAATTAGTTGCCTTTATCTCAGCCATACCAGTAACACTTGGTGTTAGAGGT AAACAAGTGCCTAGTGTAGAAATCAATTTCTTGTGCGTTCACAAACAGCTAAGATCGAAG AGATTAACACCTGTTCTAATTAAAGAAATTACGAGACGAGTGAACAAATGTGACATCTGG CATGCATTGTACACGGCAGGTATTGTTTTGCCAGCACCTGTGAGTACGTGTCGTTATACT CATCGTCCCTTGAATTGGAAGAAACTTTATGAAGTAGATTTCACAGGGTTACCAGATGGG CACACAGAGGAGGATATGATTGCTGAGAATGCGTTACCGGCCAAAACAAAGACAGCGGGA TTGAGAAAATTAAAGAAGGAAGATATTGACCAAGTTTTTGAGTTGTTCAAAAGATATCAA TCCAGGTTCGAACTAATTCAAATTTTCACAAAAGAAGAATTCGAACATAATTTCATTGGT GAAGAATCGTTACCATTGGATAAACAAGTAATTTTCTCATATGTAGTCGAACAGCCCGAT GGAAAAATTACAGACTTCTTCTCATTTTACTCATTGCCATTCACAATCCTAAATAACACA AAATATAAGGACCTAGGCATCGGGTACTTGTATTATTATGCCACCGATGCAGATTTCCAA TTCAAAGACAGGTTTGATCCAAAAGCTACTAAGGCTTTGAAAACAAGATTGTGTGAATTG ATTTATGACGCTTGTATTTTGGCCAAAAACGCTAATATGGATGTTTTTAACGCGTTGACT TCGCAAGATAATACATTGTTCTTGGATGATTTGAAGTTCGGGCCCGGTGACGGGTTCTTG AACTTCTATTTATTTAATTATAGAGCAAAGCCGATTACCGGTGGCTTGAATCCCGACAAT AGTAACGACATTAAAAGGCGTAGCAATGTCGGTGTTGTTATGTTGTAG
Protein Properties
Pfam Domain Function
Protein Residues455
Protein Molecular Weight52837.10156
Protein Theoretical pI7.49
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Glycylpeptide N-tetradecanoyltransferase MSEEDKAKKLENLLKLLQLNNDDTSKFTQEQKKAMKDHKFWRTQPVKDFDEKVVEEGPID KPKTPEDISDKPLPLLSSFEWCSIDVDNKKQLEDVFVLLNENYVEDRDAGFRFNYTKEFF NWALKSPGWKKDWHIGVRVKETQKLVAFISAIPVTLGVRGKQVPSVEINFLCVHKQLRSK RLTPVLIKEITRRVNKCDIWHALYTAGIVLPAPVSTCRYTHRPLNWKKLYEVDFTGLPDG HTEEDMIAENALPAKTKTAGLRKLKKEDIDQVFELFKRYQSRFELIQIFTKEEFEHNFIG EESLPLDKQVIFSYVVEQPDGKITDFFSFYSLPFTILNNTKYKDLGIGYLYYYATDADFQ FKDRFDPKATKALKTRLCELIYDACILAKNANMDVFNALTSQDNTLFLDDLKFGPGDGFL NFYLFNYRAKPITGGLNPDNSNDIKRRSNVGVVML
References
External Links
ResourceLink
Saccharomyces Genome Database NMT1
Uniprot IDP14743
Uniprot NameNMT_YEAST
GenBank Gene IDM23726
Genebank Protein ID172045
PDB ID
1IID
General Reference
  • Duronio, R. J., Towler, D. A., Heuckeroth, R. O., Gordon, J. I. (1989). "Disruption of the yeast N-myristoyl transferase gene causes recessive lethality." Science 243:796-800.2644694
  • Johnston, M., Hillier, L., Riles, L., Albermann, K., Andre, B., Ansorge, W., Benes, V., Bruckner, M., Delius, H., Dubois, E., Dusterhoft, A., Entian, K. D., Floeth, M., Goffeau, A., Hebling, U., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hilger, F., Kleine, K., Kotter, P., Louis, E. J., Messenguy, F., Mewes, H. W., Hoheisel, J. D., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Nature 387:87-90.9169871
  • Towler, D. A., Adams, S. P., Eubanks, S. R., Towery, D. S., Jackson-Machelski, E., Glaser, L., Gordon, J. I. (1987). "Purification and characterization of yeast myristoyl CoA:protein N-myristoyltransferase." Proc Natl Acad Sci U S A 84:2708-2712.3106975
  • Duronio, R. J., Rudnick, D. A., Johnson, R. L., Johnson, D. R., Gordon, J. I. (1991). "Myristic acid auxotrophy caused by mutation of S. cerevisiae myristoyl-CoA:protein N-myristoyltransferase." J Cell Biol 113:1313-1330.2045414
  • Johnson, D. R., Duronio, R. J., Langner, C. A., Rudnick, D. A., Gordon, J. I. (1993). "Genetic and biochemical studies of a mutant Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase, nmt72pLeu99-->Pro, that produces temperature-sensitive myristic acid auxotrophy." J Biol Chem 268:483-494.8416952
  • Rudnick, D. A., Rocque, W. J., McWherter, C. A., Toth, M. V., Jackson-Machelski, E., Gordon, J. I. (1993). "Use of photoactivatable peptide substrates of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase (Nmt1p) to characterize a myristoyl-CoA-Nmt1p-peptide ternary complex and to provide evidence for an ordered reaction mechanism." Proc Natl Acad Sci U S A 90:1087-1091.8430078
  • Zhang, L., Jackson-Machelski, E., Gordon, J. I. (1996). "Biochemical studies of Saccharomyces cerevisiae myristoyl-coenzyme A:protein N-myristoyltransferase mutants." J Biol Chem 271:33131-33140.8955162
  • Farazi, T. A., Manchester, J. K., Waksman, G., Gordon, J. I. (2001). "Pre-steady-state kinetic studies of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase mutants identify residues involved in catalysis." Biochemistry 40:9177-9186.11478885
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Bhatnagar, R. S., Futterer, K., Farazi, T. A., Korolev, S., Murray, C. L., Jackson-Machelski, E., Gokel, G. W., Gordon, J. I., Waksman, G. (1998). "Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs." Nat Struct Biol 5:1091-1097.9846880
  • Farazi, T. A., Waksman, G., Gordon, J. I. (2001). "Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis." Biochemistry 40:6335-6343.11371195