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Database: UniProt
Entry: ARGA_SALTY
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ID   ARGA_SALTY              Reviewed;         443 AA.
AC   Q8ZMB8;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 120.
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; OrderedLocusNames=STM2992;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE006468; AAL21868.1; -; Genomic_DNA.
DR   PIR; S12388; S12388.
DR   RefSeq; NP_461909.1; NC_003197.2.
DR   RefSeq; WP_000588964.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZMB8; -.
DR   SMR; Q8ZMB8; -.
DR   STRING; 99287.STM2992; -.
DR   PaxDb; 99287-STM2992; -.
DR   GeneID; 1254515; -.
DR   KEGG; stm:STM2992; -.
DR   PATRIC; fig|99287.12.peg.3166; -.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   OMA; KRKYNWD; -.
DR   PhylomeDB; Q8ZMB8; -.
DR   BioCyc; SENT99287:STM2992-MONOMER; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001014; Chromosome.
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   CDD; cd04301; NAT_SF; 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   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_0000186805"
FT   DOMAIN          296..443
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   443 AA;  49278 MW;  7400B522E653EAD9 CRC64;
     MIKERKTELV EGFRHSVPYI NTHRGKTFVI MLGGEAIEHD NFSSIVSDIG LLHSLGIRLV
     VVYGARPQID ANLAAHHHEP IYHKNTRVTD AKALELVKQA AGLLQLDITA RLSMSLNNTP
     LQGAHINVVS GNFTIAQPLG VDDGVDYCHS GRIRRIDEDA INRQLDNGAI VLMGPVAVSV
     TGESFNLTSE EIATQLAVKL KAEKMIGFCS SQGVTNSEGG IISELFPNEA QARVEELEAQ
     GDYNSGTVRF LRGAVKACRS GVRRCHLISY QEDGSLLQEL FSRDGIGTQI VMESAEQIRR
     ATINDIGGIL ELIRPLEQQG ILVRRSREQL EMEIDKFTII QRDNMTIACA ALYPFVEEKI
     GEMACVAVHP DYRSSSRGEV LLERVAAQAR QMGLRKLFVL TTRSIHWFQE RGFTPVDIEL
     LPESKKKMYN YQRRSKVLMA DLG
//
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