NATA1_ARATH
ID NATA1_ARATH Reviewed; 228 AA.
AC Q9ZV05; Q93XX7;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=L-ornithine N5-acetyltransferase NATA1;
DE EC=2.3.1.-;
DE AltName: Full=Protein N-ACETYLTRANSFERASE ACTIVITY 1;
GN Name=NATA1; OrderedLocusNames=At2g39030; ORFNames=T7F6.20;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21917546; DOI=10.1105/tpc.111.088989;
RA Adio A.M., Casteel C.L., De Vos M., Kim J.H., Joshi V., Li B., Juery C.,
RA Daron J., Kliebenstein D.J., Jander G.;
RT "Biosynthesis and defensive function of N?-acetylornithine, a jasmonate-
RT induced Arabidopsis metabolite.";
RL Plant Cell 23:3303-3318(2011).
CC -!- FUNCTION: Acetyltransferase that converts ornithine to N5-
CC acetylornithine, which is likely used in plant defense.
CC {ECO:0000269|PubMed:21917546}.
CC -!- INDUCTION: By methyl jasmonate, and wounding by the aphid M.persicae,
CC and the lepidopteran herbivores P.rapae (white cabbage butterfly) and
CC P.xylostella (diamondback moth). {ECO:0000269|PubMed:21917546}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are unable to produce N5-acetylornithine
CC in response to methyl jasmonate. {ECO:0000269|PubMed:21917546}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK96852.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC005770; AAC79613.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09628.1; -; Genomic_DNA.
DR EMBL; AY054661; AAK96852.1; ALT_FRAME; mRNA.
DR EMBL; AY072467; AAL66882.1; -; mRNA.
DR PIR; C84812; C84812.
DR RefSeq; NP_565898.1; NM_129460.4.
DR AlphaFoldDB; Q9ZV05; -.
DR SMR; Q9ZV05; -.
DR BioGRID; 3828; 9.
DR IntAct; Q9ZV05; 5.
DR STRING; 3702.AT2G39030.1; -.
DR PaxDb; Q9ZV05; -.
DR PRIDE; Q9ZV05; -.
DR ProteomicsDB; 251036; -.
DR EnsemblPlants; AT2G39030.1; AT2G39030.1; AT2G39030.
DR GeneID; 818489; -.
DR Gramene; AT2G39030.1; AT2G39030.1; AT2G39030.
DR KEGG; ath:AT2G39030; -.
DR Araport; AT2G39030; -.
DR TAIR; locus:2064930; AT2G39030.
DR eggNOG; KOG3216; Eukaryota.
DR HOGENOM; CLU_013985_41_0_1; -.
DR InParanoid; Q9ZV05; -.
DR OMA; RVEWIVI; -.
DR OrthoDB; 1228251at2759; -.
DR PhylomeDB; Q9ZV05; -.
DR BioCyc; ARA:AT2G39030-MON; -.
DR BioCyc; MetaCyc:AT2G39030-MON; -.
DR PRO; PR:Q9ZV05; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZV05; baseline and differential.
DR Genevisible; Q9ZV05; AT.
DR GO; GO:0008080; F:N-acetyltransferase activity; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006591; P:ornithine metabolic process; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039534; NATA1-like.
DR PANTHER; PTHR10545:SF59; PTHR10545:SF59; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Plant defense; Reference proteome; Transferase.
FT CHAIN 1..228
FT /note="L-ornithine N5-acetyltransferase NATA1"
FT /id="PRO_0000423400"
FT DOMAIN 77..227
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153..155
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 161..166
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 192..195
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
SQ SEQUENCE 228 AA; 25821 MW; FC7218FFD6EF778F CRC64;
MAPPTAAPEP NTVPETSPTG HRMFSRIRLA TPTDVPFIHK LIHQMAVFER LTHLFVATES
GLASTLFNSR PFQAVTVFLL EISPSPFPTT HDASSPDFTP FLETHKVDLP IEDPDREKFL
PDKLNDVVVA GFVLFFPNYP SFLAKQGFYI EDIFMREPYR RKGFGKLLLT AVAKQAVKLG
VGRVEWIVID WNVNAINFYE QMGAQVFKEW RLCRLTGDAL QAIDKLNI
