NMT_EMENI
ID NMT_EMENI Reviewed; 493 AA.
AC Q8TFN1; C8V6J4; Q5B6J1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase;
DE EC=2.3.1.97 {ECO:0000269|PubMed:12455958};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase;
DE Short=NMT;
DE AltName: Full=Peptide N-myristoyltransferase;
GN Name=swoF; Synonyms=nmt1; ORFNames=AN3839;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ASP-370, AND
RP CATALYTIC ACTIVITY.
RX PubMed=12455958; DOI=10.1128/ec.1.2.241-248.2002;
RA Shaw B.D., Momany C., Momany M.;
RT "Aspergillus nidulans swoF encodes an N-myristoyl transferase.";
RL Eukaryot. Cell 1:241-248(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular proteins. {ECO:0000269|PubMed:12455958}.
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:12455958};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL14203.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA59104.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY057437; AAL14203.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000062; EAA59104.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF75267.1; -; Genomic_DNA.
DR RefSeq; XP_661443.1; XM_656351.1.
DR AlphaFoldDB; Q8TFN1; -.
DR SMR; Q8TFN1; -.
DR STRING; 162425.CADANIAP00004867; -.
DR EnsemblFungi; CBF75267; CBF75267; ANIA_03839.
DR EnsemblFungi; EAA59104; EAA59104; AN3839.2.
DR GeneID; 2873262; -.
DR KEGG; ani:AN3839.2; -.
DR VEuPathDB; FungiDB:AN3839; -.
DR eggNOG; KOG2779; Eukaryota.
DR HOGENOM; CLU_022882_2_0_1; -.
DR InParanoid; Q8TFN1; -.
DR OMA; RDWHVGV; -.
DR OrthoDB; 1025421at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; IMP:AspGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:AspGD.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; ISM:AspGD.
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; Reference proteome; Transferase.
FT CHAIN 1..493
FT /note="Glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000064241"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 493
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000250"
FT BINDING 82..85
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 216..218
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 224..228
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT MUTAGEN 370
FT /note="D->Y: Causes a temperature sensitive growth defect."
FT /evidence="ECO:0000269|PubMed:12455958"
SQ SEQUENCE 493 AA; 56419 MW; 3EAFEA4EC8A66A32 CRC64;
MSDSKDSKGK APQKPNDAEQ TPGGKLTPQA AEALLENNPS LKNELGGLDK DKALEALRKM
DISELLTGLS LTGKNKKDMA AFKFWQTQPV PRFDEAASNA AGGPIKMIDP EKVSKEPDAL
IEGFEWTTLD LTNEEELREL WDLLTYHYVE DDNAMFRFRY SKSFLHWALM SPGWRKEWHV
GVRATKSRKL VASISGVPTQ IRVRGQKIKV TEINFLCIHK KLRSKRLAPV LIKEITRRCY
LNGIYQAIYT AGVVLPTPVS SCRYYHRPLD WLKLYEVGFS PLPRGSTKAR QITKNHLPSH
TSTPNLRPME AKDVDAVHDL LERYLNQFDI HQAFTREEID HWLVYKESPQ KEQVIWSYVV
EDPETHKITD FFSFYNLEST VIQHPKHDCV RAAYLYYYAT ETAFLDDQKA LKNRLQMLMN
DALILAKKAQ FDVFNALTSH HNPLFLEQLK FGAGDGQLHF YLYNYRTAPI AGGVNEKNLP
DENRMGGVGV VML
