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Protein

Glycylpeptide N-tetradecanoyltransferase

Gene

NMT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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.

Catalytic activityi

Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.

Enzyme regulationi

Inhibited by diethylpyrocarbonate. Competitively inhibited by S-(2-oxo)pentadecyl-CoA, a non hydrolysable myristoyl-CoA analog, and by SC-58272, a peptidomimetic derived from the N-terminal sequence of a natural substrate.

Kineticsi

  1. KM=1.4 µM for myristoyl-CoA2 Publications

    pH dependencei

    Optimum pH is 7.5-8.0.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei455Proton acceptor; via carboxylate1

    GO - Molecular functioni

    • glycylpeptide N-tetradecanoyltransferase activity Source: SGD

    GO - Biological processi

    • N-terminal peptidyl-glycine N-myristoylation Source: SGD
    • replicative cell aging Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciYEAST:YLR195C-MONOMER.
    BRENDAi2.3.1.97. 984.
    ReactomeiR-SCE-2514859. Inactivation, recovery and regulation of the phototransduction cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycylpeptide N-tetradecanoyltransferase (EC:2.3.1.97)
    Alternative name(s):
    Cell division control protein 72
    Myristoyl-CoA:protein N-myristoyltransferase
    Short name:
    NMT
    Peptide N-myristoyltransferase
    Gene namesi
    Name:NMT1
    Synonyms:CDC72
    Ordered Locus Names:YLR195C
    ORF Names:L8167.14
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XII

    Organism-specific databases

    EuPathDBiFungiDB:YLR195C.
    SGDiS000004185. NMT1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi99L → P in NMT1-72; temperature-sensitive mutant with myristic acid auxotrophy. 1 Publication1
    Mutagenesisi169N → L: Reduces the chemical transformation rate; when associated with A-205. 1 Publication1
    Mutagenesisi170F → A: Reduces the chemical transformation rate; when associated with A-171. 1 Publication1
    Mutagenesisi171L → A: Reduces the chemical transformation rate; when associated with A-170. 1 Publication1
    Mutagenesisi202A → T: Reduces affinity for both substrate and myristoyl-CoA. 1 Publication1
    Mutagenesisi205T → A: Reduces the chemical transformation rate; when associated with L-169. 1 Publication1
    Mutagenesisi217C → R: Reduces affinity for substrate, but not for myristoyl-CoA. 1 Publication1
    Mutagenesisi328S → P: Moderately reduces affinity for myristoyl-CoA, but not for substrate. 1 Publication1
    Mutagenesisi404N → Y: Moderately reduces affinity for substrate, but not for myristoyl-CoA. 1 Publication1
    Mutagenesisi426N → I: Reduces affinity for myristoyl-CoA, but not for substrate. 1 Publication1
    Mutagenesisi451G → D in NMT1-181; temperature-sensitive with myristic acid auxotrophy. Reduces affinity for myristoyl-CoA. 1 Publication1
    Mutagenesisi454 – 455Missing : Reduces chemical transformation rate 400-fold. 1 Publication2

    Chemistry databases

    ChEMBLiCHEMBL5484.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000642481 – 455Glycylpeptide N-tetradecanoyltransferaseAdd BLAST455

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    MaxQBiP14743.
    PRIDEiP14743.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi31465. 46 interactors.
    MINTiMINT-4495316.

    Chemistry databases

    BindingDBiP14743.

    Structurei

    Secondary structure

    1455
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi6 – 17Combined sources12
    Helixi35 – 37Combined sources3
    Helixi41 – 43Combined sources3
    Beta strandi57 – 60Combined sources4
    Helixi65 – 67Combined sources3
    Beta strandi79 – 83Combined sources5
    Beta strandi86 – 88Combined sources3
    Helixi89 – 102Combined sources14
    Beta strandi103 – 105Combined sources3
    Helixi107 – 109Combined sources3
    Beta strandi111 – 113Combined sources3
    Helixi117 – 124Combined sources8
    Helixi131 – 133Combined sources3
    Beta strandi134 – 139Combined sources6
    Turni140 – 142Combined sources3
    Beta strandi145 – 158Combined sources14
    Beta strandi161 – 173Combined sources13
    Helixi175 – 177Combined sources3
    Beta strandi179 – 181Combined sources3
    Helixi183 – 195Combined sources13
    Turni196 – 198Combined sources3
    Beta strandi202 – 208Combined sources7
    Beta strandi214 – 225Combined sources12
    Helixi226 – 231Combined sources6
    Helixi239 – 241Combined sources3
    Helixi243 – 250Combined sources8
    Beta strandi261 – 263Combined sources3
    Helixi266 – 268Combined sources3
    Helixi269 – 280Combined sources12
    Beta strandi283 – 287Combined sources5
    Helixi291 – 298Combined sources8
    Beta strandi301 – 303Combined sources3
    Helixi306 – 308Combined sources3
    Beta strandi311 – 317Combined sources7
    Beta strandi323 – 331Combined sources9
    Beta strandi334 – 336Combined sources3
    Beta strandi343 – 345Combined sources3
    Beta strandi347 – 355Combined sources9
    Turni357 – 360Combined sources4
    Helixi367 – 390Combined sources24
    Beta strandi394 – 400Combined sources7
    Helixi404 – 406Combined sources3
    Turni407 – 412Combined sources6
    Beta strandi414 – 425Combined sources12
    Beta strandi434 – 436Combined sources3
    Beta strandi440 – 442Combined sources3
    Turni444 – 446Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1IICX-ray2.20A/B34-455[»]
    1IIDX-ray2.50A34-455[»]
    2NMTX-ray2.90A34-455[»]
    2P6EX-ray2.90A/B/C/D/E/F1-455[»]
    2P6FX-ray3.10A/B/C/D/E/F1-455[»]
    2P6GX-ray3.00A/B/C/D/E/F1-455[»]
    ProteinModelPortaliP14743.
    SMRiP14743.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14743.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni38 – 41Myristoyl CoA-binding4
    Regioni168 – 204Myristoyl CoA-bindingAdd BLAST37

    Sequence similaritiesi

    Belongs to the NMT family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000017837.
    HOGENOMiHOG000189123.
    InParanoidiP14743.
    KOiK00671.
    OMAiNEREIWQ.
    OrthoDBiEOG092C3LZ4.

    Family and domain databases

    Gene3Di3.40.630.30. 2 hits.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000903. MyristoylCoA_TrFase.
    IPR022677. MyristoylCoA_TrFase_C.
    IPR022678. MyristoylCoA_TrFase_CS.
    IPR022676. MyristoylCoA_TrFase_N.
    [Graphical view]
    PANTHERiPTHR11377. PTHR11377. 1 hit.
    PfamiPF01233. NMT. 1 hit.
    PF02799. NMT_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015892. N-myristl_transf. 1 hit.
    SUPFAMiSSF55729. SSF55729. 2 hits.
    PROSITEiPS00975. NMT_1. 1 hit.
    PS00976. NMT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14743-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSEEDKAKKL ENLLKLLQLN NDDTSKFTQE QKKAMKDHKF WRTQPVKDFD
    60 70 80 90 100
    EKVVEEGPID KPKTPEDISD KPLPLLSSFE WCSIDVDNKK QLEDVFVLLN
    110 120 130 140 150
    ENYVEDRDAG FRFNYTKEFF NWALKSPGWK KDWHIGVRVK ETQKLVAFIS
    160 170 180 190 200
    AIPVTLGVRG KQVPSVEINF LCVHKQLRSK RLTPVLIKEI TRRVNKCDIW
    210 220 230 240 250
    HALYTAGIVL PAPVSTCRYT HRPLNWKKLY EVDFTGLPDG HTEEDMIAEN
    260 270 280 290 300
    ALPAKTKTAG LRKLKKEDID QVFELFKRYQ SRFELIQIFT KEEFEHNFIG
    310 320 330 340 350
    EESLPLDKQV IFSYVVEQPD GKITDFFSFY SLPFTILNNT KYKDLGIGYL
    360 370 380 390 400
    YYYATDADFQ FKDRFDPKAT KALKTRLCEL IYDACILAKN ANMDVFNALT
    410 420 430 440 450
    SQDNTLFLDD LKFGPGDGFL NFYLFNYRAK PITGGLNPDN SNDIKRRSNV

    GVVML
    Length:455
    Mass (Da):52,838
    Last modified:April 1, 1990 - v1
    Checksum:i0424CA3978F76AE6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M23726 Genomic DNA. Translation: AAA34815.1.
    U14913 Genomic DNA. Translation: AAB67436.1.
    BK006945 Genomic DNA. Translation: DAA09514.1.
    PIRiA40163.
    RefSeqiNP_013296.1. NM_001182082.1.

    Genome annotation databases

    EnsemblFungiiYLR195C; YLR195C; YLR195C.
    GeneIDi850892.
    KEGGisce:YLR195C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M23726 Genomic DNA. Translation: AAA34815.1.
    U14913 Genomic DNA. Translation: AAB67436.1.
    BK006945 Genomic DNA. Translation: DAA09514.1.
    PIRiA40163.
    RefSeqiNP_013296.1. NM_001182082.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1IICX-ray2.20A/B34-455[»]
    1IIDX-ray2.50A34-455[»]
    2NMTX-ray2.90A34-455[»]
    2P6EX-ray2.90A/B/C/D/E/F1-455[»]
    2P6FX-ray3.10A/B/C/D/E/F1-455[»]
    2P6GX-ray3.00A/B/C/D/E/F1-455[»]
    ProteinModelPortaliP14743.
    SMRiP14743.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31465. 46 interactors.
    MINTiMINT-4495316.

    Chemistry databases

    BindingDBiP14743.
    ChEMBLiCHEMBL5484.

    Proteomic databases

    MaxQBiP14743.
    PRIDEiP14743.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYLR195C; YLR195C; YLR195C.
    GeneIDi850892.
    KEGGisce:YLR195C.

    Organism-specific databases

    EuPathDBiFungiDB:YLR195C.
    SGDiS000004185. NMT1.

    Phylogenomic databases

    GeneTreeiENSGT00390000017837.
    HOGENOMiHOG000189123.
    InParanoidiP14743.
    KOiK00671.
    OMAiNEREIWQ.
    OrthoDBiEOG092C3LZ4.

    Enzyme and pathway databases

    BioCyciYEAST:YLR195C-MONOMER.
    BRENDAi2.3.1.97. 984.
    ReactomeiR-SCE-2514859. Inactivation, recovery and regulation of the phototransduction cascade.

    Miscellaneous databases

    EvolutionaryTraceiP14743.
    PROiP14743.

    Family and domain databases

    Gene3Di3.40.630.30. 2 hits.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000903. MyristoylCoA_TrFase.
    IPR022677. MyristoylCoA_TrFase_C.
    IPR022678. MyristoylCoA_TrFase_CS.
    IPR022676. MyristoylCoA_TrFase_N.
    [Graphical view]
    PANTHERiPTHR11377. PTHR11377. 1 hit.
    PfamiPF01233. NMT. 1 hit.
    PF02799. NMT_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015892. N-myristl_transf. 1 hit.
    SUPFAMiSSF55729. SSF55729. 2 hits.
    PROSITEiPS00975. NMT_1. 1 hit.
    PS00976. NMT_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiNMT_YEAST
    AccessioniPrimary (citable) accession number: P14743
    Secondary accession number(s): D6VYJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: November 2, 2016
    This is version 162 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Has an ordered Bi-Bi kinetic mechanism, with myristoyl-CoA binding taking place prior to peptide binding and CoA release occurring before acylated peptide release. Cooperative interactions between the acyl-CoA and peptide binding sites of NMT contribute to its extraordinary chain-length specificity.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.