NMT2_ARATH
ID NMT2_ARATH Reviewed; 430 AA.
AC Q94L32; O80586;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative glycylpeptide N-tetradecanoyltransferase 2;
DE EC=2.3.1.97;
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase 2;
DE Short=NMT 2;
DE Short=Type I N-myristoyltransferase 2;
DE AltName: Full=Peptide N-myristoyltransferase 2;
GN Name=NMT2; OrderedLocusNames=At2g44170; ORFNames=F6E13.30;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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).
CC -!- FUNCTION: May add a myristoyl group to the N-terminal glycine residue
CC of certain cellular proteins. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23421.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF250957; AAK49038.1; -; mRNA.
DR EMBL; AC004005; AAC23421.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T00697; T00697.
DR AlphaFoldDB; Q94L32; -.
DR SMR; Q94L32; -.
DR PeptideAtlas; Q94L32; -.
DR PRIDE; Q94L32; -.
DR Araport; AT2G44170; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q94L32; baseline and differential.
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.
PE 5: Uncertain;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..430
FT /note="Putative glycylpeptide N-tetradecanoyltransferase 2"
FT /id="PRO_0000064232"
FT ACT_SITE 430
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000250"
FT BINDING 47..50
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 181..183
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 189..193
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
SQ SEQUENCE 430 AA; 49628 MW; 08F2333ED0E23035 CRC64;
MSDPKLKPVE DALVTVAKSS QIQLAKDDTS GGTIVGRLLQ CQYSKTHKFW ETQPVEQFKD
IQDTSLPEGP IEPATLVSEV KQEPYNLLGQ FEWTICDMNS DDMCLEMYNF LKENSPDDQQ
IKYEYSKEYL RWALCPPGYY QSWHIGVRVK TSKKLIAFIC GRPTRIRVRD EVVKMAKVNS
LCVHKKLRSK GLAPLMIKEL TRRVKLQNIW QAAYTSSHIL SRPVTTSRDW VRMLNPKKLI
DVGLTRLRDR MTMSRTVKLY KLPDAPITPG FREMERRDVP AVTALLRNYL SQFAVATDFD
DNDVKHWLLP RENIVYSYVV VSPETHDVTD FCSFCNSSIT IPGNRKYTTL ECAYACCNVA
TLTSLSQLVN DALIVSKQKG FDVFYASDVM QNESFLKELR FYPLCRQSHY YLYNYRLRNA
LKPSELGLIL