ID   ARGA_PSEPU              Reviewed;         432 AA.
AC   P0A100; P32042;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
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;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PPN;
RA   Dharmsthiti S., Krishnapillai V.;
RL   Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=M38359; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M38359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_003253723.1; NZ_SPUU01000008.1.
DR   AlphaFoldDB; P0A100; -.
DR   SMR; P0A100; -.
DR   STRING; 1240350.AMZE01000032_gene2146; -.
DR   eggNOG; COG0548; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   OMA; KRKYNWD; -.
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_0000186800"
FT   DOMAIN          286..432
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   432 AA;  47440 MW;  BFB889B705F22450 CRC64;
     MPDYVNWLRH ASPYINAHRD CTFVVMLPGD GVEHPNFGNI VHDLVLLHSL GVRLVLVHGS
     RPQIESRLAD RGLTPHYHRG MRITDAATLD CVIDAVGALR LAIEARLSMD IAASPMQGSR
     LRVASGNLVT ARPIGVLEGV DYHHTGEVRR VDRKGISRLL DERSIVLLSP LGYSPTGEIF
     NLACEDVATR AAIELGADKL LLFGAEPGLL DADGRLVREL RPQQVAPHLQ RLGSDYQGEL
     LDAAAEACKG GVARSHIVSY AEDGALLTEL FTRGGGGTLV SQEQFEVVRE ATIEDVGGLL
     ELISPLEEQG ILVRRSREVL EREIEQFSVV EREGMIIACA ALYPIADSEA GELACLAVNP
     EYRHGGRGDE LLERIESRAR QMGLSTLFVL TTRTAHWFRE RGFAPSGVER LPAARASLYN
     YQRNSKIFEK PL