NMT_PLAF7
ID NMT_PLAF7 Reviewed; 410 AA.
AC Q8ILW6; A0A144A366;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase;
DE EC=2.3.1.97 {ECO:0000250|UniProtKB:Q9U419};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase {ECO:0000250|UniProtKB:Q9U419};
DE AltName: Full=N-myristoyltransferase {ECO:0000303|PubMed:34695132};
GN Name=NMT {ECO:0000303|PubMed:34695132}; ORFNames=PF14_0127, PF3D7_1412800;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP FUNCTION.
RX PubMed=34695132; DOI=10.1371/journal.pbio.3001408;
RA Schlott A.C., Knuepfer E., Green J.L., Hobson P., Borg A.J.,
RA Morales-Sanfrutos J., Perrin A.J., Maclachlan C., Collinson L.M.,
RA Snijders A.P., Tate E.W., Holder A.A.;
RT "Inhibition of protein N-myristoylation blocks Plasmodium falciparum
RT intraerythrocytic development, egress and invasion.";
RL PLoS Biol. 19:e3001408-e3001408(2021).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular proteins (By similarity). Myristoylates adenylate
CC kinase AK2 (By similarity). During the asexual blood stage, may
CC myristoylate proteins such as ARO, CDPK1 and GAP45 (PubMed:34695132).
CC Probably by mediating protein myristoylation, plays a role in the
CC assembly of the inner membrane complex during the early stages of
CC schizogony and in the formation of rhoptries in the late stages and
CC thus merozoite egress (PubMed:34695132). {ECO:0000250|UniProtKB:Q9U419,
CC ECO:0000269|PubMed:34695132}.
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:0000250|UniProtKB:Q9U419};
CC -!- SUBUNIT: Heterodimer composed of NMT and AK2; AK2 myristoylation
CC stabilizes the complex. {ECO:0000250|UniProtKB:Q9U419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30419}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR EMBL; LN999946; CZT99838.1; -; Genomic_DNA.
DR RefSeq; XP_001348300.1; XM_001348264.1.
DR AlphaFoldDB; Q8ILW6; -.
DR SMR; Q8ILW6; -.
DR STRING; 5833.PF14_0127; -.
DR BindingDB; Q8ILW6; -.
DR ChEMBL; CHEMBL2169722; -.
DR GuidetoPHARMACOLOGY; 2955; -.
DR SwissPalm; Q8ILW6; -.
DR PRIDE; Q8ILW6; -.
DR EnsemblProtists; CZT99838; CZT99838; PF3D7_1412800.
DR GeneID; 811708; -.
DR KEGG; pfa:PF3D7_1412800; -.
DR VEuPathDB; PlasmoDB:PF3D7_1412800; -.
DR HOGENOM; CLU_022882_0_1_1; -.
DR InParanoid; Q8ILW6; -.
DR OMA; RDWHVGV; -.
DR PhylomeDB; Q8ILW6; -.
DR BRENDA; 2.3.1.97; 4889.
DR Proteomes; UP000001450; Chromosome 14.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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..410
FT /note="Glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000064230"
FT BINDING 30
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 31
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 162
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 163
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 164
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 165
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 171
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 173
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 174
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 175
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
SQ SEQUENCE 410 AA; 47970 MW; AA823DD100D80C10 CRC64;
MNDDKKDFVG RDLYQLIRNA KDKIKIDYKF WYTQPVPKIN DEFDENVNEP FISDNKVEDV
RKEEYKLPSG YAWCVCDITK ENDRSDIYNL LTDNYVEDDD NVFRFNYSSE FLLWALSSPN
YVKNWHIGVK YESTNKLVGF ISAIPIDMCV NKNIIKMAEV NFLCVHKSLR SKRLAPVLIK
EITRRINLES IWQAIYTAGV YLPKPISTAR YFHRSINVKK LIEIGFSCLN TRLTMSRAIK
LYRIDDTLNI KNLRLMKKKD IDGLQKLLNE HLKQYNLHAI FSKEDVAHWF TPIDQVIYTY
VNEENGEIKD LISFYSLPSK VLGNNKYNIL NAAFSFYNIT TTTTFKNLIQ DAICLAKRNN
FDVFNALEVM DNYSVFQDLK FGEGDGSLKY YLYNWKCASC HPSKIGIVLL
