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NMT_ASHGO
ID   NMT_ASHGO               Reviewed;         452 AA.
AC   Q75EK2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Glycylpeptide N-tetradecanoyltransferase;
DE            EC=2.3.1.97;
DE   AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase;
DE            Short=NMT;
DE   AltName: Full=Peptide N-myristoyltransferase;
GN   Name=NMT1; OrderedLocusNames=AAR077C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC       certain cellular proteins. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) +
CC         N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-
CC         COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723,
CC         ChEBI:CHEBI:133050; EC=2.3.1.97;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR   EMBL; AE016814; AAS50442.1; -; Genomic_DNA.
DR   RefSeq; NP_982618.1; NM_207971.1.
DR   AlphaFoldDB; Q75EK2; -.
DR   SMR; Q75EK2; -.
DR   STRING; 33169.AAS50442; -.
DR   EnsemblFungi; AAS50442; AAS50442; AGOS_AAR077C.
DR   GeneID; 4618539; -.
DR   KEGG; ago:AGOS_AAR077C; -.
DR   eggNOG; KOG2779; Eukaryota.
DR   HOGENOM; CLU_022882_2_0_1; -.
DR   InParanoid; Q75EK2; -.
DR   OMA; RDWHVGV; -.
DR   Proteomes; UP000000591; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; IBA:GO_Central.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000903; NMT.
DR   InterPro; IPR022677; NMT_C.
DR   InterPro; IPR022678; NMT_CS.
DR   InterPro; IPR022676; NMT_N.
DR   PANTHER; PTHR11377; PTHR11377; 1.
DR   Pfam; PF01233; NMT; 1.
DR   Pfam; PF02799; NMT_C; 1.
DR   PIRSF; PIRSF015892; N-myristl_transf; 1.
DR   SUPFAM; SSF55729; SSF55729; 2.
DR   PROSITE; PS00975; NMT_1; 1.
DR   PROSITE; PS00976; NMT_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..452
FT                   /note="Glycylpeptide N-tetradecanoyltransferase"
FT                   /id="PRO_0000064234"
FT   ACT_SITE        452
FT                   /note="Proton acceptor; via carboxylate"
FT                   /evidence="ECO:0000250"
FT   BINDING         38..41
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   BINDING         171..173
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   BINDING         179..183
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
SQ   SEQUENCE   452 AA;  52754 MW;  2B11E19DFA50097F CRC64;
     MGDSGDAQKM QRLLEMLALN SGDMSKLTQQ QRKAFEEYKF WKTQPVARFD EKVEEEGPIN
     PPRRVEDVRD EPYPLLEEFE WRTMDITTGQ DLEDVFVLLN ENYIEDKDST FRFNYTREFF
     NWALKPPGWR KEWHVGVRVR QSGRLVAFIS AVPTTLEVRG REMKSVEINF LCIHKKLRSK
     RLAPILIKEI TRRVNKCDIW HALYSAGIVL PSPISTCRYT HRPLNWSKLF DVGFTALPAN
     ATKTQMLAKY TLPKKPLVEG LRPMTDADVD GAFDLFNRYQ KRFELIQTFD KSEFRHWFLG
     NEETPSVIYS YVVQNSEGKI TDFVSFYSLP FTILKNPLHK ELGIGYLFYY ASDADFDYED
     RYDPTATELL RKRLTQLIND VCILARDLKM DVFNALTSQD NALFLEDLKF GPGDGFLNFY
     LFNYRANPIR GGLTEDKKFD AKNRSNQGVV ML
 
 
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