ID   ARGA_ESCF3              Reviewed;         443 AA.
AC   B7LW98;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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}; OrderedLocusNames=EFER_0252;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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         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; CU928158; CAQ87821.1; -; Genomic_DNA.
DR   RefSeq; WP_000238002.1; NC_011740.1.
DR   AlphaFoldDB; B7LW98; -.
DR   SMR; B7LW98; -.
DR   EnsemblBacteria; CAQ87821; CAQ87821; EFER_0252.
DR   GeneID; 60903450; -.
DR   KEGG; efe:EFER_0252; -.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   OMA; KRKYNWD; -.
DR   OrthoDB; 901370at2; -.
DR   BioCyc; EFER585054:EFER_RS01470-MON; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000745; 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   Transferase.
FT   CHAIN           1..443
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_1000137050"
FT   DOMAIN          296..434
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
SQ   SEQUENCE   443 AA;  49096 MW;  1B6BA86085DBB4B9 CRC64;
     MVKERSTELV QGFRHSVPYI NTHRGKTFVI MLGGEAIEHE NFSSIVNDIG LLHSLGIRLV
     VVYGARPQID ANLAAHQHEP LYHKNIRVTD AKTLELVKQA AGTLQLDITA RLSMSLNNTP
     LQGAHINVVS GNFIIAQPLG VDDGVDYCHS GRIRRIDEEA IHRQLDSGAI VLLGPVAVSV
     TGESFNLTSE EIATQLAIKL KAEKMIGFCS SQGVTNDDGD IVSELFPNEA QARVEAQETA
     GDYNSGTVRF LRGAVKACRS GVRRCHLISY QEDGALLQEL FSRDGIGTQI VMESAEQIRR
     ATINDIGGIL ELIRPLEQQG ILVRRSREQL EMEIDKFTII QRDNTTIACA ALYPFPEEKI
     GEMACVAVHP DYRSSARGEV LLERIAAQAK QIGLSKLFVL TTRSIHWFQE RGFTPVDIDL
     LPESKKLMYN YQRRSKVLMA DLG