ID   ARGA_PSEAE              Reviewed;         432 AA.
AC   P22567;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 142.
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=PA5204;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PAO;
RA   Dharmsthiti S., Krishnapillai V.V.;
RL   Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(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   -!- INTERACTION:
CC       P22567; P22567: argA; NbExp=2; IntAct=EBI-6418319, EBI-6418319;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA73977.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M38358; AAA73977.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE004091; AAG08589.1; -; Genomic_DNA.
DR   PIR; G82995; G82995.
DR   PIR; S27600; S27600.
DR   RefSeq; NP_253891.1; NC_002516.2.
DR   RefSeq; WP_003096265.1; NZ_QZGE01000002.1.
DR   AlphaFoldDB; P22567; -.
DR   SMR; P22567; -.
DR   STRING; 287.DR97_2573; -.
DR   PaxDb; P22567; -.
DR   PRIDE; P22567; -.
DR   EnsemblBacteria; AAG08589; AAG08589; PA5204.
DR   GeneID; 879475; -.
DR   KEGG; pae:PA5204; -.
DR   PATRIC; fig|208964.12.peg.5454; -.
DR   PseudoCAP; PA5204; -.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   InParanoid; P22567; -.
DR   OMA; KRKYNWD; -.
DR   PhylomeDB; P22567; -.
DR   BioCyc; PAER208964:G1FZ6-5323-MON; -.
DR   BRENDA; 2.3.1.1; 5087.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000002438; 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:0004358; F:glutamate N-acetyltransferase activity; IMP:PseudoCAP.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IMP:PseudoCAP.
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   1: Evidence at protein level;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Reference proteome; Transferase.
FT   CHAIN           1..432
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_0000186798"
FT   DOMAIN          286..425
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   432 AA;  47859 MW;  725FAD778FD44A4E CRC64;
     MPDYVNWLRH ASPYINSHRD RTFVVMLPGE GVEHPNFGNI VHDLVLLHSL GARLVLVHGS
     RPQIEARLAA RGLAPRYHRD LRVTDAPTLE CVIDAVGSLR IAIEARLSMD MAASPMQGAR
     LRVAGGNLVT ARPIGVVEGV DYHHTGEVRR IDRKGIGRLL DERSIVLLSP LGYSPTGEIF
     NLACEDVAMR AAIDLEAEKL ILYGAEQGLL DASGKLVREL RPQQVPAHLQ RLGNSYQAEL
     LDAAAQACRA GVKRSHIVSY TEDGALLSEL FTRTGNGTLV AQEQFEQLRE AGIEDVGGLI
     ELIRPLEEQG ILVRRSREVL EREIEQFSIV EREGLIIACA ALYPIADSEA GELACLAVNP
     EYRHGGRGDE LLERIEERAR GLGLKTLFVL TTRTAHWFRE RGFQPSSVER LPAARASLYN
     FQRNSQVFEK SL