ID   ARGA_VIBCH              Reviewed;         445 AA.
AC   Q9KPQ0;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 2.
DT   25-MAY-2022, entry version 102.
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=VC_2316;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF95460.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE003852; AAF95460.1; ALT_INIT; Genomic_DNA.
DR   PIR; E82093; E82093.
DR   RefSeq; NP_231947.1; NC_002505.1.
DR   AlphaFoldDB; Q9KPQ0; -.
DR   SMR; Q9KPQ0; -.
DR   STRING; 243277.VC_2316; -.
DR   DNASU; 2613112; -.
DR   EnsemblBacteria; AAF95460; AAF95460; VC_2316.
DR   KEGG; vch:VC_2316; -.
DR   PATRIC; fig|243277.26.peg.2207; -.
DR   eggNOG; COG0548; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   OMA; KRKYNWD; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000584; Chromosome 1.
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..445
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_0000186808"
FT   DOMAIN          299..445
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   445 AA;  49443 MW;  A3C1B1EE0591F182 CRC64;
     MKIRSTALVK GFRQSAPYVN AHRGKTMVVM LGGEAIADKN FPNIISDIAL LHSLGVKVVL
     VHGARPQINQ ILEKNQRDTP YHKGVRITDE SSLGLVMQAA GQLQHAITAR LSMSLNNTPM
     AGTQLNVVSG NFIISQPLGI DEGVDYCHSG RIRRIDVEGI NRMLDLGSIV LLGPIASSVT
     GECFNLLSEE VATQVAIKLK ADKLIGFCPQ QGIIDTKGNA IAELFPSDVE RLVKSMEQEC
     APDDEECFST MRFLRAALKA CRAGVPRSHL VSYKEDGALI QELFSFDGIG TQIVMASAEQ
     IRQATIDDIG GIFDLIRPLE EQGILVRRSR EQLEQEIHKF TIIDKDGLVI GCSALYPYPE
     ERMAEMACVA IHPEYRDGHR GLHLLVHSKH QAKQMGIRHL FVLTTHSTHW FREQGFNEVD
     VEALPMAKKS LYNYQRRSKI LMLQL