NMT_CANAL
ID NMT_CANAL Reviewed; 451 AA.
AC P30418; A0A1D8PLA8; Q5AMK5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase;
DE EC=2.3.1.97 {ECO:0000269|PubMed:1569105, ECO:0000269|PubMed:8300631, ECO:0000269|PubMed:9115247};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase;
DE Short=NMT;
DE AltName: Full=Peptide N-myristoyltransferase;
GN Name=NMT1; OrderedLocusNames=CAALFM_C401440WA;
GN ORFNames=CaO19.12111, CaO19.4641;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 121-132; 291-300;
RP 341-359 AND 408-423, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 32354 / B311;
RX PubMed=1569105; DOI=10.1016/s0021-9258(18)42484-2;
RA Wiegand R.C., Carr C., Minnerly J.C., Pauley A.M., Carron C.P.,
RA Langner C.A., Duronio R.J., Gordon J.I.;
RT "The Candida albicans myristoyl-CoA:protein N-myristoyltransferase gene.
RT Isolation and expression in Saccharomyces cerevisiae and Escherichia
RT coli.";
RL J. Biol. Chem. 267:8591-8598(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP FUNCTION, MUTAGENESIS OF GLY-447, AND CATALYTIC ACTIVITY.
RX PubMed=8300631; DOI=10.1016/s0021-9258(17)42038-2;
RA Lodge J.K., Johnson R.L., Weinberg R.A., Gordon J.I.;
RT "Comparison of myristoyl-CoA:protein N-myristoyltransferases from three
RT pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and
RT Candida albicans.";
RL J. Biol. Chem. 269:2996-3009(1994).
RN [6]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=9115247; DOI=10.1074/jbc.272.18.11874;
RA McWherter C.A., Rocque W.J., Zupec M.E., Freeman S.K., Brown D.L.,
RA Devadas B., Getman D.P., Sikorski J.A., Gordon J.I.;
RT "Scanning alanine mutagenesis and de-peptidization of a Candida albicans
RT myristoyl-CoA:protein N-myristoyltransferase octapeptide substrate reveals
RT three elements critical for molecular recognition.";
RL J. Biol. Chem. 272:11874-11880(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RX PubMed=9501915; DOI=10.1038/nsb0398-213;
RA Weston S.A., Camble R., Colls J., Rosenbrock G., Taylor I., Egerton M.,
RA Tucker A.D., Tunnicliffe A., Mistry A., Mancia F., de la Fortelle E.,
RA Irwin J., Bricogne G., Pauptit R.A.;
RT "Crystal structure of the anti-fungal target N-myristoyl transferase.";
RL Nat. Struct. Biol. 5:213-221(1998).
RN [8] {ECO:0007744|PDB:1IYK, ECO:0007744|PDB:1IYL}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 60-451 IN COMPLEXES WITH
RP MYRISTOYL-COA AND INHIBITORS.
RX PubMed=12401496; DOI=10.1016/s1074-5521(02)00240-5;
RA Sogabe S., Masubuchi M., Sakata K., Fukami T.A., Morikami K., Shiratori Y.,
RA Ebiike H., Kawasaki K., Aoki Y., Shimma N., D'Arcy A., Winkler F.K.,
RA Banner D.W., Ohtsuka T.;
RT "Crystal structures of Candida albicans N-myristoyltransferase with two
RT distinct inhibitors.";
RL Chem. Biol. 9:1119-1128(2002).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular proteins. Substrate specificity requires an N-terminal
CC glycine in the nascent polypeptide substrates. Ser is present at
CC position 5 in almost all known N-myristoyl proteins and Lys is commonly
CC encountered at postion 6. Basic residues are preferred at positions 7
CC and 8. {ECO:0000269|PubMed:1569105, ECO:0000269|PubMed:8300631,
CC ECO:0000269|PubMed:9115247}.
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 Evidence={ECO:0000269|PubMed:1569105, ECO:0000269|PubMed:8300631,
CC ECO:0000269|PubMed:9115247};
CC -!- ACTIVITY REGULATION: Competitively inhibited by SC-58272, a
CC peptidomimetic derived from the N-terminal sequence of a natural
CC substrate.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12401496}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Has an ordered Bi-Bi kinetic mechanism, with myristoyl-
CC CoA binding taking place prior to peptide binding and CoA release
CC occurring before acylated peptide release. Cooperative interactions
CC between the acyl-CoA and peptide binding sites of NMT contribute to its
CC extraordinary chain-length specificity.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR EMBL; M80544; AAA34351.1; -; Genomic_DNA.
DR EMBL; CP017626; AOW28926.1; -; Genomic_DNA.
DR PIR; A38099; A38099.
DR RefSeq; XP_722713.1; XM_717620.2.
DR PDB; 1IYK; X-ray; 2.30 A; A/B=60-451.
DR PDB; 1IYL; X-ray; 3.20 A; A/B/C/D=60-451.
DR PDB; 1NMT; X-ray; 2.45 A; A/B/C=60-451.
DR PDBsum; 1IYK; -.
DR PDBsum; 1IYL; -.
DR PDBsum; 1NMT; -.
DR AlphaFoldDB; P30418; -.
DR SMR; P30418; -.
DR BioGRID; 1218551; 1.
DR STRING; 237561.P30418; -.
DR BindingDB; P30418; -.
DR ChEMBL; CHEMBL3548; -.
DR DrugBank; DB03062; (1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanone.
DR DrugBank; DB02180; Myristoyl-Coa.
DR DrugBank; DB02477; N-({4-[4-(2-Methyl-1H-imidazol-1-yl)butyl]phenyl}acetyl)-L-seryl-N-(2-cyclohexylethyl)-L-lysinamide.
DR PRIDE; P30418; -.
DR GeneID; 3635624; -.
DR KEGG; cal:CAALFM_C401440WA; -.
DR CGD; CAL0000201559; NMT1.
DR VEuPathDB; FungiDB:C4_01440W_A; -.
DR eggNOG; KOG2779; Eukaryota.
DR HOGENOM; CLU_022882_1_0_1; -.
DR InParanoid; P30418; -.
DR OMA; RDWHVGV; -.
DR OrthoDB; 1025421at2759; -.
DR BRENDA; 2.3.1.97; 1096.
DR EvolutionaryTrace; P30418; -.
DR PRO; PR:P30418; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IDA:CGD.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; IDA:CGD.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Transferase.
FT CHAIN 1..451
FT /note="Glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000064236"
FT ACT_SITE 451
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000250"
FT BINDING 177..179
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:12401496,
FT ECO:0007744|PDB:1IYK"
FT BINDING 185..189
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:12401496,
FT ECO:0007744|PDB:1IYK"
FT MUTAGEN 447
FT /note="G->D: Causes temperature-dependent reduction in
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:8300631"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1IYK"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 149..162
FT /evidence="ECO:0007829|PDB:1IYK"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 167..179
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1IYL"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:1IYK"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 220..231
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 314..322
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:1IYK"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:1IYK"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:1IYK"
FT TURN 402..407
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 409..420
FT /evidence="ECO:0007829|PDB:1IYK"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:1IYK"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:1IYK"
SQ SEQUENCE 451 AA; 51863 MW; 7D106E2C08D5922D CRC64;
MSGDNTGNKS NSAPSKSIEE LLKLLAMGQE LSPAQQKEMK DYKFWKTQPV PSLSETVTEE
GPIDKLKTPE DVPNDPLPLI SDFEWSTLDI DDNLQLDELY KLLYDNYVED IDATFRFKYS
HEFFQWALKP PGWRKDWHVG VRVKSTGKLV AFIAATPVTF KLNKSNKVID SVEINFLCIH
KKLRNKRLAP VLIKEITRRV NKQNIWQALY TGGSILPTPL TTCRYQHRPI NWSKLHDVGF
SHLPPNQTKS SMVASYTLPN NPKLKGLRPM TGKDVSTVLS LLYKYQERFD IVQLFTEEEF
KHWMLGHDEN SDSNVVKSYV VEDENGVITD YFSYYLLPFT VLDNAQHDEL GIAYLFYYAS
DSFEKPNYKK RLNELITDAL ITSKKFGVDV FNCLTCQDNT YFLKDCKFGS GDGFLNYYLF
NYRTFPMDGG IDKKTKEVVE DQTSGIGVVL L
