ID   ARGA_SHIFL              Reviewed;         443 AA.
AC   P59293;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 1.
DT   25-MAY-2022, entry version 119.
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=SF2829, S3026;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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   -!- ACTIVITY REGULATION: Feedback inhibition by L-arginine. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE005674; AAN44316.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18141.1; -; Genomic_DNA.
DR   RefSeq; NP_708609.2; NC_004337.2.
DR   RefSeq; WP_000237959.1; NZ_UIQL01000014.1.
DR   AlphaFoldDB; P59293; -.
DR   SMR; P59293; -.
DR   STRING; 198214.SF2829; -.
DR   EnsemblBacteria; AAN44316; AAN44316; SF2829.
DR   EnsemblBacteria; AAP18141; AAP18141; S3026.
DR   GeneID; 1025049; -.
DR   KEGG; sfl:SF2829; -.
DR   KEGG; sft:NCTC1_03114; -.
DR   KEGG; sfx:S3026; -.
DR   PATRIC; fig|198214.7.peg.3367; -.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   OMA; KRKYNWD; -.
DR   OrthoDB; 901370at2; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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..443
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_0000186807"
FT   DOMAIN          296..443
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   443 AA;  49209 MW;  6A3C3EDF90170B47 CRC64;
     MVKERKTELV EGFRHSVPYI NTHRGKTFVI MLGGEAIEHE NFSSIVNDIG LLHSLGIRLV
     VVYGARPQID ANLAAHHHEP LYHKNIRVTD AKTLELVKQA AGTLQLDITA RLSMSLNNTP
     LQGAHINVVS GNFIIAQPLG VDDGVDYCHS GRIRRIDEDA LHRQLESGAI VLMGPVAVSV
     TGESFNLTSE EIATQLAIKL KAEKMIGFCS SQGVTNDDGD IVSELFPNEA QARVEAQEEK
     GDYNSGTVRF LRGAVKACRS GVRRCHLISY QEDGALLQEL FSRDGIGTQI VMESAEQIRR
     ATINDIGGIL ELIRPLEQQG ILVRRSREQL EMEIDKFTII QRDNTTIACA ALYPFPEEKI
     GEMACVAVHP DYRSSSRGEV LLERIAAQAK QSGLSKLFVL TTRSIHWFQE RGFTPVDIDL
     LPESKKQLYN YQRKSKVLMA DLG