NMT1_ARATH
ID NMT1_ARATH Reviewed; 434 AA.
AC Q9LTR9; Q9M6E3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase 1;
DE EC=2.3.1.97 {ECO:0000269|PubMed:10734119, ECO:0000269|PubMed:12912986};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase 1;
DE Short=NMT 1;
DE Short=Type I N-myristoyltransferase 1;
DE AltName: Full=Peptide N-myristoyltransferase 1;
GN Name=NMT1; OrderedLocusNames=At5g57020; ORFNames=MHM17.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=10734119; DOI=10.1074/jbc.275.13.9673;
RA Qi Q., Rajala R.V.S., Anderson W., Jiang C., Rozwadowski K., Selvaraj G.,
RA Sharma R., Datla R.;
RT "Molecular cloning, genomic organization, and biochemical characterization
RT of myristoyl-CoA:protein N-myristoyltransferase from Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 275:9673-9683(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12912986; DOI=10.1074/jbc.m307321200;
RA Boisson B., Giglione C., Meinnel T.;
RT "Unexpected protein families including cell defense components feature in
RT the N-myristoylome of a higher eukaryote.";
RL J. Biol. Chem. 278:43418-43429(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular proteins. Can also use decanoyl-CoA and lauroyl-CoA as
CC substrates. {ECO:0000269|PubMed:10734119, ECO:0000269|PubMed:12912986}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 uM for myristoyl-CoA, in the presence of CPK3
CC {ECO:0000269|PubMed:10734119};
CC pH dependence:
CC Optimum pH is 7.8. Active from pH 5.5 to 8.5.
CC {ECO:0000269|PubMed:10734119};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10734119}.
CC Note=Mostly associated to ribosomes. Present to a lower extent in
CC mitochondria.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, with higher levels in young
CC tissues (at protein level). {ECO:0000269|PubMed:10734119}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97032.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF193616; AAF60968.1; -; mRNA.
DR EMBL; AF250956; AAK49037.1; -; mRNA.
DR EMBL; AB024035; BAA97032.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96835.1; -; Genomic_DNA.
DR EMBL; AY045854; AAK76528.1; -; mRNA.
DR EMBL; AY091380; AAM14319.1; -; mRNA.
DR EMBL; AY087547; AAM65089.1; -; mRNA.
DR RefSeq; NP_568846.1; NM_125084.3.
DR AlphaFoldDB; Q9LTR9; -.
DR SMR; Q9LTR9; -.
DR BioGRID; 21049; 1.
DR STRING; 3702.AT5G57020.1; -.
DR iPTMnet; Q9LTR9; -.
DR PaxDb; Q9LTR9; -.
DR PRIDE; Q9LTR9; -.
DR ProteomicsDB; 251069; -.
DR EnsemblPlants; AT5G57020.1; AT5G57020.1; AT5G57020.
DR GeneID; 835805; -.
DR Gramene; AT5G57020.1; AT5G57020.1; AT5G57020.
DR KEGG; ath:AT5G57020; -.
DR Araport; AT5G57020; -.
DR TAIR; locus:2164580; AT5G57020.
DR eggNOG; KOG2779; Eukaryota.
DR HOGENOM; CLU_022882_0_1_1; -.
DR OMA; RDWHVGV; -.
DR OrthoDB; 1025421at2759; -.
DR PhylomeDB; Q9LTR9; -.
DR BRENDA; 2.3.1.97; 399.
DR PRO; PR:Q9LTR9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTR9; baseline and differential.
DR Genevisible; Q9LTR9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005840; C:ribosome; IDA:TAIR.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IDA:TAIR.
DR GO; GO:0019107; F:myristoyltransferase activity; IDA:TAIR.
DR GO; GO:0010064; P:embryonic shoot morphogenesis; IMP:TAIR.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; IBA:GO_Central.
DR GO; GO:0006499; P:N-terminal protein myristoylation; IDA:TAIR.
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 Acetylation; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..434
FT /note="Glycylpeptide N-tetradecanoyltransferase 1"
FT /id="PRO_0000064231"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 434
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000250"
FT BINDING 48..51
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 184..186
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 192..196
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 434 AA; 49799 MW; 778138CBF91525D4 CRC64;
MADNNSPPGS VEQKADQIVE ANPLVKDDTS LETIVRRFQD SMSEAKTHKF WETQPVGQFK
DIGDTSLPEG PIEPATPLSE VKQEPYNLPS VYEWTTCDMN SDDMCSEVYN LLKNNYVEDD
ENMFRFNYSK EFLRWALRPP GYYQSWHIGV RAKTSKKLVA FISGVPARIR VRDEVVKMAE
INFLCVHKKL RSKRLAPVMI KEVTRRVHLE NIWQAAYTAG VILPTPITTC QYWHRSLNPK
KLIDVGFSRL GARMTMSRTI KLYKLPDAPI TPGFRKMEPR DVPAVTRLLR NYLSQFGVAT
DFDENDVEHW LLPREDVVDS YLVESPETHD VTDFCSFYTL PSTILGNPNY TTLKAAYSYY
NVATQTSFLQ LMNDALIVSK QKGFDVFNAL DVMHNESFLK ELKFGPGDGQ LHYYLYNYRL
KSALKPAELG LVLL
