NMT_ASPFU
ID NMT_ASPFU Reviewed; 492 AA.
AC Q9UVX3; Q4WP53;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
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; ORFNames=AFUA_4G08070;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sakata K., Hashido K., Aoki Y., Arisawa M.;
RT "N-myristoyl transferase.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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}.
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DR EMBL; AB035414; BAA87865.1; -; mRNA.
DR EMBL; AAHF01000005; EAL89981.1; -; Genomic_DNA.
DR RefSeq; XP_752019.1; XM_746926.1.
DR PDB; 4CAV; X-ray; 1.89 A; A=86-492.
DR PDB; 4CAW; X-ray; 2.50 A; A=86-492.
DR PDB; 4CAX; X-ray; 1.85 A; A=86-492.
DR PDB; 4QBJ; X-ray; 2.10 A; A=101-492.
DR PDB; 4UWI; X-ray; 1.80 A; A=86-492.
DR PDB; 4UWJ; X-ray; 1.70 A; A=86-492.
DR PDB; 5T5U; X-ray; 1.80 A; A=86-492.
DR PDB; 5T6C; X-ray; 1.90 A; A=86-492.
DR PDB; 5T6E; X-ray; 2.30 A; A=86-492.
DR PDB; 5T6H; X-ray; 1.80 A; A=86-492.
DR PDBsum; 4CAV; -.
DR PDBsum; 4CAW; -.
DR PDBsum; 4CAX; -.
DR PDBsum; 4QBJ; -.
DR PDBsum; 4UWI; -.
DR PDBsum; 4UWJ; -.
DR PDBsum; 5T5U; -.
DR PDBsum; 5T6C; -.
DR PDBsum; 5T6E; -.
DR PDBsum; 5T6H; -.
DR AlphaFoldDB; Q9UVX3; -.
DR SMR; Q9UVX3; -.
DR STRING; 746128.CADAFUBP00006342; -.
DR BindingDB; Q9UVX3; -.
DR ChEMBL; CHEMBL3988591; -.
DR PRIDE; Q9UVX3; -.
DR EnsemblFungi; EAL89981; EAL89981; AFUA_4G08070.
DR GeneID; 3508953; -.
DR KEGG; afm:AFUA_4G08070; -.
DR VEuPathDB; FungiDB:Afu4g08070; -.
DR eggNOG; KOG2779; Eukaryota.
DR HOGENOM; CLU_022882_2_0_1; -.
DR InParanoid; Q9UVX3; -.
DR OMA; RDWHVGV; -.
DR OrthoDB; 1025421at2759; -.
DR BRENDA; 2.3.1.97; 508.
DR Proteomes; UP000002530; Chromosome 4.
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; 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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..492
FT /note="Glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000064235"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 492
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 215..217
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 223..227
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:4CAV"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:4UWJ"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 189..202
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 205..217
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4CAW"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 258..269
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 335..342
FT /evidence="ECO:0007829|PDB:4UWJ"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:4UWJ"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 366..382
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 387..399
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 407..427
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:4UWJ"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:4UWJ"
FT TURN 444..449
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 451..465
FT /evidence="ECO:0007829|PDB:4UWJ"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:4CAX"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:5T5U"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:4UWJ"
SQ SEQUENCE 492 AA; 56255 MW; 921C0C5FF805F000 CRC64;
MSDSKDRKGK APEGQSSEKK DGAVNITPQM AESLLENNPA LRNETAGMDK DKAAEAMRKM
NIAELLTGLS VSGKNQKDMA SYKFWQTQPV PRFDETSTDT GGPIKIIDPE KVSKEPDALL
EGFEWATLDL TNETELQELW DLLTYHYVED DNAMFRFRYS QSFLHWALMS PGWKKEWHVG
VRATKSRKLV ASICGVPTEI NVRNQKLKVV EINFLCIHKK LRSKRLTPVL IKEITRRCYL
NGIYQAIYTA GVVLPTPVSS CRYYHRPLDW LKLYEVGFSP LPAGSTKARQ ITKNHLPSTT
STPGLRPMEP KDIDTVHDLL QRYLSRFALN QAFTREEVDH WLVHKPETVK EQVVWAYVVE
DPETHKITDF FSFYNLESTV IQNPKHDNVR AAYLYYYATE TAFTNNMKAL KERLLMLMND
ALILAKKAHF DVFNALTLHD NPLFLEQLKF GAGDGQLHFY LYNYRTAPVP GGVNEKNLPD
EKRMGGVGIV ML
