ID   ARGA_PSESY              Reviewed;         432 AA.
AC   P61919;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Amino-acid acetyltransferase;
DE            EC=2.3.1.1;
DE   AltName: Full=N-acetylglutamate synthase;
DE            Short=AGS;
DE            Short=NAGS;
GN   Name=argA; Synonyms=syrA;
OS   Pseudomonas syringae pv. syringae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B301D;
RX   PubMed=14660376; DOI=10.1128/aem.69.12.7273-7280.2003;
RA   Lu S.E., Soule J.D., Gross D.C.;
RT   "Characterization of the argA gene required for arginine biosynthesis and
RT   syringomycin production by Pseudomonas syringae pv. syringae.";
RL   Appl. Environ. Microbiol. 69:7273-7280(2003).
RN   [2]
RP   IMPORTANCE FOR PATHOGENICITY.
RX   PubMed=2848010; DOI=10.1128/jb.170.12.5680-5688.1988;
RA   Xu G.W., Gross D.C.;
RT   "Physical and functional analyses of the syrA and syrB genes involved in
RT   syringomycin production by Pseudomonas syringae pv. syringae.";
RL   J. Bacteriol. 170:5680-5688(1988).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: A functional ArgA is critical for the production of the
CC       phytotoxin syringomycin and, therefore, for pathogenicity in plants.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY374326; AAQ82442.1; -; Genomic_DNA.
DR   RefSeq; WP_003403912.1; NZ_QPCD01000104.1.
DR   AlphaFoldDB; P61919; -.
DR   SMR; P61919; -.
DR   UniPathway; UPA00068; UER00106.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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; 2.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   PIRSF; PIRSF000423; ArgA; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR01890; N-Ac-Glu-synth; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Transferase.
FT   CHAIN           1..432
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_0000186802"
FT   DOMAIN          286..425
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   432 AA;  47916 MW;  831D913FCB1C357A CRC64;
     MPEYVNWLRH ASPYINAHRD CTFVVMLPGD GVAHPNFGNI VHDLVLLHSL GVRLVLVHGS
     RPQIESRLAQ RGITPRYHRD LRITDTETLE CVIDAVGQLR ISIEARLSMD MAASPMQGSR
     LRVTSGNVVT ARPIGVLEGV DYQHTGEVRR VDRKGINRLL DERHIVLLSP LGYSPTGEIF
     NLACEDVATR AAIDLAADKL LLFGAETGLL DEQGRLVREL RPQQVPAHLQ RLGANYQAEL
     LDAAAEACRG GVARSHIVSY AENGALLTEL FTRDGGGTLV AQEQFELVRE AAIEDVGGLM
     DLITPLEEQG ILVRRSREVL EREITQFSVV EREGLIIACA ALYPIADSES GELACLAVNP
     EYRHGGRGDE LLERIENRAR ALGIKTLFVL TTRTAHWFRE RGFEPSSVDR LPSARASLYN
     YQRNSKIFEK AI