NMT_CANGA
ID NMT_CANGA Reviewed; 451 AA.
AC O74234; Q6FY92;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
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=CAGL0A04059g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hosking S.L., Massey S.E., Egerton M.;
RT "Isolation of the gene encoding the myristoyl-CoA:protein N-
RT myristoyltransferase from the pathogenic yeast, Candida glabrata.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular proteins.
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.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC26048.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF073886; AAC26048.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CR380947; CAG57836.1; -; Genomic_DNA.
DR RefSeq; XP_444943.1; XM_444943.1.
DR AlphaFoldDB; O74234; -.
DR SMR; O74234; -.
DR STRING; 5478.XP_444943.1; -.
DR EnsemblFungi; CAG57836; CAG57836; CAGL0A04059g.
DR GeneID; 2886412; -.
DR KEGG; cgr:CAGL0A04059g; -.
DR CGD; CAL0126631; NMT1.
DR VEuPathDB; FungiDB:CAGL0A04059g; -.
DR eggNOG; KOG2779; Eukaryota.
DR HOGENOM; CLU_022882_2_0_1; -.
DR InParanoid; O74234; -.
DR OMA; RDWHVGV; -.
DR Proteomes; UP000002428; Chromosome A.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006499; P:N-terminal protein myristoylation; IEA:InterPro.
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..451
FT /note="Glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000064237"
FT ACT_SITE 451
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000250"
FT BINDING 34..37
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 167..169
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 175..179
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT CONFLICT 338
FT /note="Y -> F (in Ref. 1; AAC26048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 52659 MW; 514364B1FE3A2CC9 CRC64;
MSEKKIEELL KLLSMNNGDM SKLTANQRKE MKEYKFWKTQ PVTKFDEEVK EEGPIHEEKT
PADIPDEPLP LLPDFEWCAI DVDDEKQLED VFVLLNENYV EDRDASFRFN YTREFFNWAL
KSPGWTPDWH IGVRVKASKK LIAFISAIPV RLRVRAKVID SVEINFLCVH KQLRSKRLTP
VLIKEITRRV NKRNIWHALY TAGVVLPAPV STCRYAHRPL NWDKLYEVQF TDLPPNATKA
EMVAKYTLPK ATKTAGLREL RLEDVDQALA LFNRYQSRFD IVQEFTKEEF IHWFINDKNV
VEQDKRVVFS YVVESEGKVT DFFSFYSLPF TILNNSRYKD LGIGYLYYYA SDADFKFEDR
FDKEGTSLLK QRLSTLVQDA CIIAAQNKMD VFNALSSQDN TLFLEDLKFG PGDGFLNFYL
FNYRTFPITG GLTEDQHFDT EHRSNVGVVM L
