ID   ARGA_SALAR              Reviewed;         443 AA.
AC   A9MS91;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 87.
DE   RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01105};
DE            EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01105};
DE   AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01105};
DE            Short=AGS {ECO:0000255|HAMAP-Rule:MF_01105};
DE            Short=NAGS {ECO:0000255|HAMAP-Rule:MF_01105};
GN   Name=argA {ECO:0000255|HAMAP-Rule:MF_01105};
GN   OrderedLocusNames=SARI_04668;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+);
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01105};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01105}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01105}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01105}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01105}.
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DR   EMBL; CP000880; ABX24435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9MS91; -.
DR   SMR; A9MS91; -.
DR   STRING; 41514.SARI_04668; -.
DR   KEGG; ses:SARI_04668; -.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0004042; F:L-glutamate N-acetyltransferase activity, acting on acetyl-CoA as donor; IEA:UniProtKB-UniRule.
DR   GO; GO:0004358; F:L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor; IEA:UniProtKB-ARBA.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04237; AAK_NAGS-ABP; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   FunFam; 3.40.1160.10:FF:000005; Amino-acid acetyltransferase; 1.
DR   FunFam; 3.40.630.30:FF:000009; Amino-acid acetyltransferase; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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   NCBIfam; TIGR01890; N-Ac-Glu-synth; 1.
DR   NCBIfam; NF003641; PRK05279.1; 1.
DR   PANTHER; PTHR30602; AMINO-ACID ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR30602:SF12; AMINO-ACID ACETYLTRANSFERASE NAGS1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   PIRSF; PIRSF000423; ArgA; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Reference proteome; Transferase.
FT   CHAIN           1..443
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_1000084822"
FT   DOMAIN          296..436
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
SQ   SEQUENCE   443 AA;  49358 MW;  24E15E72B0FF1FB8 CRC64;
     MIKERRTELV EGFRHSVPYI NTHRGKTFVI MLGGEAIEHD NFSSIVNDIG LLHSLGIRLV
     VVYGARPQID ANLAAHHHEP IYHKNTRVTD AKTLELVKQA AGLLQLDITA RLSMSLNNTP
     LQGAHINVVS GNFTIAQPLG VDDGVDYCHS GRIRRIDEDA INRQLDNGAI VLIGPVAVSV
     TGESFNLTSE EIATQLAVKL KAEKMIGFCS SQGVTNSKGD VISELFPNEA QARVEELEAQ
     GDYNSGTVRF LRGAVKACRS GVRRCHLISY QEDGTLLQEL FSREGIGTQI VMESAEQIRR
     ATINDIGGIL ELIRPLEQQG ILVRRSREQL EMEIDKFTII QRDNMTIACA ALYPFVEEKI
     GEMACVAVHP DYRSSSRGEI LLERIAAQAR QMGLSKLFVL TTRSIHWFQE RGFTPVDIEL
     LPESKKKMYN YQRRSKVLIA DLG
//