ID   ARGA_BUCAI              Reviewed;         442 AA.
AC   O66143;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 127.
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=BU456;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-71.
RX   PubMed=9569646; DOI=10.1016/s0965-1748(97)00092-1;
RA   Nakabachi A., Ishikawa H.;
RT   "Differential display of mRNAs related to amino acid metabolism in the
RT   endosymbiotic system of aphids.";
RL   Insect Biochem. Mol. Biol. 27:1057-1062(1997).
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; BA000003; BAB13154.1; -; Genomic_DNA.
DR   EMBL; AB005263; BAA25386.1; -; mRNA.
DR   RefSeq; NP_240268.1; NC_002528.1.
DR   RefSeq; WP_009874409.1; NC_002528.1.
DR   AlphaFoldDB; O66143; -.
DR   SMR; O66143; -.
DR   STRING; 107806.10039120; -.
DR   EnsemblBacteria; BAB13154; BAB13154; BAB13154.
DR   KEGG; buc:BU456; -.
DR   PATRIC; fig|107806.10.peg.466; -.
DR   eggNOG; COG0548; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   OMA; KRKYNWD; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001806; 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; PF13508; Acetyltransf_7; 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   2: Evidence at transcript level;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Reference proteome; Transferase.
FT   CHAIN           1..442
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_0000186788"
FT   DOMAIN          295..442
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   442 AA;  49226 MW;  C7F67E99C285A394 CRC64;
     MKERNTELVQ GFRHSVPYIN AHRGKTFVIM LGGEAIKYGN FYSIINDIGL LHSLGIRLVV
     VYGACPQINT SLKEKNIKII YHKSIRITDL ASLEQVKQAA GKLQLDITAR LSMSLTNTPL
     QGANISVVSG NFIISQPLGV DDGVDYCHSG RVRRIDKNAI NCQLNNGAIV LIGPVAVSVT
     GESFNLTSEE IATQVSIELK AEKMIGFCGN QGVINDEGKI ISELLSNDIK NIIKKLEKKG
     DYISSTVRFL KGSIKACKSG VNRSHLISYH KSGALLQELF SRDGIGTQMV MESAEKIRGA
     SINDIGGILE LIRPLEHKGI LVRRSREQLE IEVDKFTIIE HDNLTIACAA LYPFFKEKIG
     EMACLAVHPD YRNSSRGDAL LKKIKMNAKD MHLKRIFVLT TQSIHWFQER GFILVDIEVL
     PESKKKMYNY QRGSKILMID VI