NMT_PLAFA
ID NMT_PLAFA Reviewed; 410 AA.
AC Q9U419;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase {ECO:0000255|RuleBase:RU000586};
DE EC=2.3.1.97 {ECO:0000255|RuleBase:RU000586, ECO:0000269|PubMed:10816442, ECO:0000269|PubMed:18973776};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase {ECO:0000303|PubMed:10816442};
DE AltName: Full=N-myristoyltransferase {ECO:0000303|PubMed:10816442};
DE Short=PfNMT {ECO:0000303|PubMed:18973776};
GN Name=NMT {ECO:0000303|PubMed:10816442};
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833 {ECO:0000312|EMBL:AAF18461.1};
RN [1] {ECO:0000312|EMBL:AAF18461.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=T9/96 {ECO:0000269|PubMed:10816442};
RX PubMed=10816442; DOI=10.1042/bj3480459;
RA Gunaratne R.S., Sajid M., Ling I.T., Tripathi R., Pachebat J.A.,
RA Holder A.A.;
RT "Characterization of N-myristoyltransferase from Plasmodium falciparum.";
RL Biochem. J. 348:459-463(2000).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH AK2.
RC STRAIN=T9/96 {ECO:0000269|PubMed:10816442};
RX PubMed=18973776; DOI=10.1016/j.molbiopara.2008.09.008;
RA Rahlfs S., Koncarevic S., Iozef R., Mailu B.M., Savvides S.N.,
RA Schirmer R.H., Becker K.;
RT "Myristoylated adenylate kinase-2 of Plasmodium falciparum forms a
RT heterodimer with myristoyltransferase.";
RL Mol. Biochem. Parasitol. 163:77-84(2009).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular proteins (PubMed:10816442, PubMed:18973776).
CC Myristoylates adenylate kinase AK2 (PubMed:18973776). During the
CC asexual blood stage, may myristoylate proteins such as ARO, CDPK1 and
CC GAP45 (By similarity). Probably by mediating protein myristoylation,
CC plays a role in the assembly of the inner membrane complex during the
CC early stages of schizogony and in the formation of rhoptries in the
CC late stages and thus merozoite egress (By similarity).
CC {ECO:0000250|UniProtKB:Q8ILW6, ECO:0000269|PubMed:10816442,
CC ECO:0000269|PubMed:18973776}.
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:0000255|RuleBase:RU000586, ECO:0000269|PubMed:10816442,
CC ECO:0000269|PubMed:18973776};
CC -!- SUBUNIT: Heterodimer composed of NMT and AK2; AK2 myristoylation
CC stabilizes the complex. {ECO:0000269|PubMed:18973776}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30419}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage.
CC {ECO:0000269|PubMed:10816442}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000255|RuleBase:RU004178}.
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; AF206306; AAF18461.1; -; Genomic_DNA.
DR SMR; Q9U419; -.
DR VEuPathDB; PlasmoDB:PF3D7_1412800; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000488000; -.
DR VEuPathDB; PlasmoDB:Pf7G8_140018200; -.
DR VEuPathDB; PlasmoDB:PfCD01_140018500; -.
DR VEuPathDB; PlasmoDB:PfDd2_140017400; -.
DR VEuPathDB; PlasmoDB:PfGA01_140018500; -.
DR VEuPathDB; PlasmoDB:PfGB4_140019000; -.
DR VEuPathDB; PlasmoDB:PfGN01_140018100; -.
DR VEuPathDB; PlasmoDB:PfHB3_140018700; -.
DR VEuPathDB; PlasmoDB:PfIT_140019400; -.
DR VEuPathDB; PlasmoDB:PfKE01_140018100; -.
DR VEuPathDB; PlasmoDB:PfKH01_140018400; -.
DR VEuPathDB; PlasmoDB:PfKH02_140018700; -.
DR VEuPathDB; PlasmoDB:PfML01_140018300; -.
DR VEuPathDB; PlasmoDB:PfNF135_140018300; -.
DR VEuPathDB; PlasmoDB:PfNF166_140017000; -.
DR VEuPathDB; PlasmoDB:PfNF54_140017800; -.
DR VEuPathDB; PlasmoDB:PfSD01_140016300; -.
DR VEuPathDB; PlasmoDB:PfSN01_140020200; -.
DR VEuPathDB; PlasmoDB:PfTG01_140018200; -.
DR OMA; RDWHVGV; -.
DR BRENDA; 2.3.1.97; 4889.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006499; P:N-terminal protein myristoylation; IDA:UniProtKB.
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 Acyltransferase; Cytoplasm; Transferase.
FT CHAIN 1..410
FT /note="Glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000455417"
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
