ID   ARGA_PASMU              Reviewed;         440 AA.
AC   Q9CMJ6;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 118.
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=PM0828;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE004439; AAK02912.1; -; Genomic_DNA.
DR   RefSeq; WP_005756904.1; NC_002663.1.
DR   AlphaFoldDB; Q9CMJ6; -.
DR   SMR; Q9CMJ6; -.
DR   STRING; 747.DR93_1668; -.
DR   EnsemblBacteria; AAK02912; AAK02912; PM0828.
DR   KEGG; pmu:PM0828; -.
DR   PATRIC; fig|272843.6.peg.838; -.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   OMA; KRKYNWD; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000809; 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   Reference proteome; Transferase.
FT   CHAIN           1..440
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_0000186796"
FT   DOMAIN          289..429
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   440 AA;  49841 MW;  600BE0D0AC4AEDDD CRC64;
     MRSTELVHWF RQSTPYVNMH RGKTFVIMLD GDTIACPNFV NIINDISLLH SLGIKLVLVF
     GARYQINELL QQHQIESVYH KNIRITDLTS LELVKQAVGK LNYDIASRLS LRLPHSPLID
     VVSGNFVLAQ PIGVDDGIDY QLSGKIRRIN TESIQQQLDR DAIVLIGPIA PSVTGESFNL
     PFEEIASQLA IKLKAEKLIG FSATQGILDE NNQTISDLLP QDAELYLAKL IQQNQYHSSQ
     ARFLQAAIEA CRFGIKRSHL ISYEEDGSLL QELFTRDGVG TQLSMEHSET IRLATVSDIP
     ALLELIRPLE QQGILVKRSR EQLEMEINQY TIIDRDGVII ACAALNCYAD EKMAEMACVA
     VHPDYRNSSR GDILLEAIQK RAKQLGIEKL FVLTTRTVHW FQERGFQLAE IADLPDKKRQ
     HYNYQRRSKI LIQALQNKKG