ID   ARGA_BUCAP              Reviewed;         442 AA.
AC   P59099;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=BUsg_441;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67984.1; -; Genomic_DNA.
DR   RefSeq; WP_011053951.1; NC_004061.1.
DR   AlphaFoldDB; P59099; -.
DR   SMR; P59099; -.
DR   STRING; 198804.BUsg_441; -.
DR   EnsemblBacteria; AAM67984; AAM67984; BUsg_441.
DR   KEGG; bas:BUsg_441; -.
DR   eggNOG; COG0548; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   OMA; KRKYNWD; -.
DR   OrthoDB; 901370at2; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000416; 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   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..442
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_0000186789"
FT   DOMAIN          295..442
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   442 AA;  49585 MW;  15074C28D9107753 CRC64;
     MRERTTELVQ GFRHSVPYIN AHRGKKFVIM LSGEAIKYGN FSGIINDIGL LHSLGIRLIV
     VYGSCPQINA NLKEKNIKIT YHKYIRVTDL LSLEQVKQAA GRLQLDITAR LSMSLSNTPL
     QGANINVVSG NFIIAQPLGV DDGIDYCHSG RIRRIDKKAI NCQLENGAIV LIGPVAVSVT
     GESFNLTSEE IATQVSIKLK AEKMIGFCSK QGVIDSQGKT ISELLPNNIQ NEIKKLEGKG
     DYISSTIRFL RGSIKACKSG VNRSHLISYH KNGALLQELF SRDGIGTQMV MESAEKIRQA
     NINDIGGILE LIRPLEKKGI LVRRSREQLE MEVDKFTIIE RDNLTIACAA LYPFFKEKIG
     EMACVAVHPD YRNSSRGDLL LQTMKLNAKK LNLKKIFVLT TQSIHWFQER GFILVDVEIL
     PESKKKMYNY QRCSKILMID LF