Glycylpeptide N-tetradecanoyltransferase
Details
- Name
- Glycylpeptide N-tetradecanoyltransferase
- Kind
- protein
- Synonyms
- 2.3.1.97
- Myristoyl-CoA:protein N-myristoyltransferase
- NMT
- Peptide N-myristoyltransferase
- Gene Name
- NMT1
- UniProtKB Entry
- P30418Swiss-Prot
- Organism
- Yeast
- NCBI Taxonomy ID
- 237561
- Amino acid sequence
>lcl|BSEQ0016450|Glycylpeptide N-tetradecanoyltransferase MSGDNTGNKSNSAPSKSIEELLKLLAMGQELSPAQQKEMKDYKFWKTQPVPSLSETVTEE GPIDKLKTPEDVPNDPLPLISDFEWSTLDIDDNLQLDELYKLLYDNYVEDIDATFRFKYS HEFFQWALKPPGWRKDWHVGVRVKSTGKLVAFIAATPVTFKLNKSNKVIDSVEINFLCIH KKLRNKRLAPVLIKEITRRVNKQNIWQALYTGGSILPTPLTTCRYQHRPINWSKLHDVGF SHLPPNQTKSSMVASYTLPNNPKLKGLRPMTGKDVSTVLSLLYKYQERFDIVQLFTEEEF KHWMLGHDENSDSNVVKSYVVEDENGIITDYFSYYLLPFTVLDNAQHDELGIAYLFYYAS DSFEKPNYKKRLNELITDALITSKKFGVDVFNCLTCQDNTYFLKDCKFGSGDGFLNYYLF NYRTFPMDGGIDKKTKEVVEDQTSGIGVVLL
- Number of residues
- 451
- Molecular Weight
- 51876.7
- Theoretical pI
- 6.44
- GO Classification
- Functionsdrug binding / glycylpeptide N-tetradecanoyltransferase activityProcessesN-terminal peptidyl-glycine N-myristoylation / pathogenesisComponentscytoplasm
- General Function
- Glycylpeptide n-tetradecanoyltransferase activity
- Specific Function
- Adds 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. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6. Basic residues are preferred at positions 7 and 8.
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0016451|Glycylpeptide N-tetradecanoyltransferase (NMT1) ATGTCGGGAGATAACACAGGGAATAAATCCAATTCAGCACCTTCAAAATCAATTGAAGAA TTGTTGAAATTATTGGCTATGGGACAAGAATTATCCCCGGCTCAACAAAAGGAAATGAAA GATTATAAATTTTGGAAGACTCAACCTGTACCATCATTAAGTGAAACCGTCACTGAAGAA GGTCCTATTGATAAATTGAAAACTCCAGAAGATGTTCCTAATGATCCATTACCATTGATC AGTGATTTTGAATGGAGTACTTTAGATATTGACGATAATTTACAATTGGATGAATTATAT AAATTATTATATGATAATTATGTTGAAGATATTGATGCCACATTTAGATTCAAATATAGT CATGAATTTTTCCAATGGGCTTTGAAACCACCGGGATGGAGAAAAGATTGGCATGTTGGG GTTAGAGTGAAATCAACTGGGAAATTAGTAGCTTTTATAGCTGCTACTCCGGTCACTTTT AAATTAAATAAATCAAATAAAGTGATTGATTCAGTGGAAATCAACTTTTTATGTATTCAT AAAAAATTAAGAAATAAGAGATTAGCCCCTGTATTAATCAAAGAAATCACTCGTAGGGTT AATAAACAAAACATTTGGCAAGCATTATATACTGGTGGATCGATTTTACCTACACCATTG ACAACTTGTCGTTATCAACATCGCCCAATCAATTGGTCGAAATTGCATGATGTGGGGTTC AGTCATTTACCTCCAAATCAAACGAAAAGCAGCATGGTGGCAAGTTATACATTACCTAAT AATCCTAAATTGAAAGGTTTACGTCCAATGACTGGGAAAGATGTTTCCACCGTATTATCT TTATTGTATAAATATCAAGAACGATTTGATATTGTACAACTTTTTACCGAAGAAGAATTT AAACATTGGATGTTGGGTCATGATGAAAATTCAGATTCTAATGTGGTTAAAAGTTATGTA GTTGAAGATGAAAATGGGGTTATTACCGATTATTTTTCATATTATTTGTTACCATTCACA GTATTAGACAATGCTCAACATGATGAATTAGGAATTGCTTATTTGTTTTATTATGCCAGT GATTCCTTTGAAAAACCAAATTATAAAAAGAGATTAAATGAATTAATCACTGATGCATTA ATTACCAGTAAAAAATTTGGAGTTGATGTTTTCAATTGTTTAACTTGTCAAGATAATACT TATTTCTTAAAAGATTGTAAATTTGGTAGTGGTGATGGTTTTTTAAATTATTATCTTTTT AATTATAGAACATTCCCTATGGATGGAGGAATTGATAAAAAGACAAAAGAAGTTGTCGAA GATCAAACAAGTGGTATAGGTGTAGTTTTATTATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P30418 UniProtKB Entry Name NMT_CANAL GenBank Protein ID 170884 GenBank Gene ID M80544 PDB ID(s) 1IYK, 1IYL, 1NMT KEGG ID cal:CaO19.12111 NCBI Gene ID 3635457 - General References
- Wiegand RC, Carr C, Minnerly JC, Pauley AM, Carron CP, Langner CA, Duronio RJ, Gordon JI: The Candida albicans myristoyl-CoA:protein N-myristoyltransferase gene. Isolation and expression in Saccharomyces cerevisiae and Escherichia coli. J Biol Chem. 1992 Apr 25;267(12):8591-8. [Article]
- Jones T, Federspiel NA, Chibana H, Dungan J, Kalman S, Magee BB, Newport G, Thorstenson YR, Agabian N, Magee PT, Davis RW, Scherer S: The diploid genome sequence of Candida albicans. Proc Natl Acad Sci U S A. 2004 May 11;101(19):7329-34. Epub 2004 May 3. [Article]
- Lodge JK, Johnson RL, Weinberg RA, Gordon JI: Comparison of myristoyl-CoA:protein N-myristoyltransferases from three pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and Candida albicans. J Biol Chem. 1994 Jan 28;269(4):2996-3009. [Article]
- McWherter CA, Rocque WJ, Zupec ME, Freeman SK, Brown DL, Devadas B, Getman DP, Sikorski JA, Gordon JI: Scanning alanine mutagenesis and de-peptidization of a Candida albicans myristoyl-CoA:protein N-myristoyltransferase octapeptide substrate reveals three elements critical for molecular recognition. J Biol Chem. 1997 May 2;272(18):11874-80. [Article]
- 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: Crystal structure of the anti-fungal target N-myristoyl transferase. Nat Struct Biol. 1998 Mar;5(3):213-21. [Article]
- Sogabe S, Masubuchi M, Sakata K, Fukami TA, Morikami K, Shiratori Y, Ebiike H, Kawasaki K, Aoki Y, Shimma N, D'Arcy A, Winkler FK, Banner DW, Ohtsuka T: Crystal structures of Candida albicans N-myristoyltransferase with two distinct inhibitors. Chem Biol. 2002 Oct;9(10):1119-28. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Myristoyl-Coa experimental unknown target Details N-({4-[4-(2-Methyl-1H-imidazol-1-yl)butyl]phenyl}acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide experimental unknown target Details (1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanone experimental unknown target Details