ID   NAGS2_ARATH             Reviewed;         613 AA.
AC   B5X4Z4;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Probable amino-acid acetyltransferase NAGS2, chloroplastic;
DE            EC=2.3.1.1;
DE   AltName: Full=N-acetylglutamate synthase 2;
DE   Flags: Precursor;
GN   Name=NAGS2; OrderedLocusNames=At4g37670; ORFNames=F19F18.160;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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;
RA   De Los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: N-acetylglutamate synthase involved in arginine biosynthesis.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC         Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4.
CC   -!- INTERACTION:
CC       B5X4Z4; Q9XGN1: TTG1; NbExp=3; IntAct=EBI-15197867, EBI-395803;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=B5X4Z4-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL035605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002687; AEE86822.1; -; Genomic_DNA.
DR   EMBL; BT046113; ACI46501.1; -; mRNA.
DR   RefSeq; NP_974701.1; NM_202972.5. [B5X4Z4-1]
DR   AlphaFoldDB; B5X4Z4; -.
DR   SMR; B5X4Z4; -.
DR   BioGRID; 15202; 3.
DR   IntAct; B5X4Z4; 3.
DR   STRING; 3702.AT4G37670.2; -.
DR   PaxDb; B5X4Z4; -.
DR   PRIDE; B5X4Z4; -.
DR   ProteomicsDB; 251020; -. [B5X4Z4-1]
DR   EnsemblPlants; AT4G37670.2; AT4G37670.2; AT4G37670. [B5X4Z4-1]
DR   GeneID; 829921; -.
DR   Gramene; AT4G37670.2; AT4G37670.2; AT4G37670. [B5X4Z4-1]
DR   KEGG; ath:AT4G37670; -.
DR   Araport; AT4G37670; -.
DR   TAIR; locus:2120130; AT4G37670.
DR   eggNOG; KOG2436; Eukaryota.
DR   HOGENOM; CLU_024773_1_0_1; -.
DR   InParanoid; B5X4Z4; -.
DR   PhylomeDB; B5X4Z4; -.
DR   UniPathway; UPA00068; UER00106.
DR   PRO; PR:B5X4Z4; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; B5X4Z4; baseline and differential.
DR   Genevisible; B5X4Z4; AT.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04237; AAK_NAGS-ABP; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   HAMAP; MF_01105; N_acetyl_glu_synth; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR033719; NAGS_kin.
DR   InterPro; IPR010167; NH2A_AcTrfase.
DR   PANTHER; PTHR30602; PTHR30602; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF53633; SSF53633; 2.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR01890; N-Ac-Glu-synth; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Amino-acid biosynthesis;
KW   Arginine biosynthesis; Chloroplast; Plastid; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..74
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           75..613
FT                   /note="Probable amino-acid acetyltransferase NAGS2,
FT                   chloroplastic"
FT                   /id="PRO_0000423407"
FT   DOMAIN          455..603
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   613 AA;  67395 MW;  0F506BE670CCF64F CRC64;
     MERGALVGSS STSSYYVPYH FRQSKSNFSS FKPKNKLNPT QFRFNCSWFK PVSSITAAKC
     NMFDYAVTAA GDVEAEHPVD DKQFVRWFRE AWPYLWAHRG CTFVVIISGE IIAGSSCDAI
     LKDIAFLHHL GIRFVLVPGT QEQIDQLLAE RGREATYVGR YRVTDAASLQ AAKEAAGAIS
     VMLEAKLSPG PSICNIRRHG DRSRLHDIGV RVDTGNFFAA KRRGVVDGVD FGATGEVKKI
     DVDRICERLD GGSVVLLRNL GHSSSGEVLN CNTYEVATAC ALAIGADKLI CIMDGPILDE
     SGHLIHFLTL QEADMLVRKR AQQSDIAANY VKAVGDGSMA YPEPPNNTNG NITSAQNGRA
     VSFWGNGNHT PIFQNGVGFD NGNGLWPCEQ GFAIGGEERL SRLNGYLSEL AAAAFVCRGG
     VKRVHLLDGT ISGVLLLELF KRDGMGTMVA SDVYEGTRDA RVEDLAGIRH IIKPLEESGI
     LVRRTDEELL RALDSFVVVE REGQIIACAA LFPFFKDKCG EVAAIAVASD CRGQGQGDKL
     LDYIEKKASS LGLEKLFLLT TRTADWFVRR GFQECSIEII PESRRQRINL SRNSKYYMKK
     LIPDRSGISV MRI