ID   ARGA_PROMH              Reviewed;         444 AA.
AC   B4F2F5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 95.
DE   RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01105};
DE            EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01105};
DE   AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01105};
DE            Short=AGS {ECO:0000255|HAMAP-Rule:MF_01105};
DE            Short=NAGS {ECO:0000255|HAMAP-Rule:MF_01105};
GN   Name=argA {ECO:0000255|HAMAP-Rule:MF_01105};
GN   OrderedLocusNames=PMI2307;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+);
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01105};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01105}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01105}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01105}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01105}.
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DR   EMBL; AM942759; CAR44559.1; -; Genomic_DNA.
DR   RefSeq; WP_004249500.1; NC_010554.1.
DR   AlphaFoldDB; B4F2F5; -.
DR   SMR; B4F2F5; -.
DR   EnsemblBacteria; CAR44559; CAR44559; PMI2307.
DR   GeneID; 6803060; -.
DR   KEGG; pmr:PMI2307; -.
DR   eggNOG; COG0548; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000008319; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0004042; F:L-glutamate N-acetyltransferase activity, acting on acetyl-CoA as donor; IEA:UniProtKB-UniRule.
DR   GO; GO:0004358; F:L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor; IEA:UniProtKB-ARBA.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04237; AAK_NAGS-ABP; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   FunFam; 3.40.1160.10:FF:000005; Amino-acid acetyltransferase; 1.
DR   FunFam; 3.40.630.30:FF:000009; Amino-acid acetyltransferase; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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   NCBIfam; TIGR01890; N-Ac-Glu-synth; 1.
DR   NCBIfam; NF003641; PRK05279.1; 1.
DR   PANTHER; PTHR30602; AMINO-ACID ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR30602:SF12; AMINO-ACID ACETYLTRANSFERASE NAGS1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   PIRSF; PIRSF000423; ArgA; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 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..444
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_1000137051"
FT   DOMAIN          295..434
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
SQ   SEQUENCE   444 AA;  49390 MW;  58C3705E0DD2684B CRC64;
     MKERSTELVD GFRHSVPYIN AHRGKTFVIM LGGEAIAHEN FPSIINDIGL LHSLGIRLVV
     VYGARPQIDV ALEEQKISPL YHKHTRITDS KTLEVVKQSA GTLQLDITAR LSMSLSNTPL
     QGAHINVVSG NFVIAQPLGV DDGVDYCHSG KIRRIDEEAI HRQLDNHAIV LIGPVAVSVT
     GESFNLTSEE VATQLAIKLK AQKLIGFCSS QGVVDASGQI VSELLPNQAE ERIQALQTTG
     DYHSGTVRFL RGAVTACRRG VERSHLLSYQ ADGAIVQELF SRDGIGTQIV MESAEKVRRA
     NINDIGGILE LIRPLEQQGI LVRRSREQLE MEIDQFTIIE RDNLTIACAA LYPYQSEKIG
     EMACVAVHPD YRSSCRGEVL LQRISTQAKQ MGLDKLFVLT TRSIHWFQEK GFTPAEIDKL
     PIEKQALYNY QRRSKILILD LHKE
//