ID   ARGA_NEIMB              Reviewed;         436 AA.
AC   Q9JXU9;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 117.
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=NMB1876;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(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   -!- MISCELLANEOUS: In bacteria which possess the bifunctional enzyme
CC       ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA
CC       fulfills an anaplerotic role.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE002098; AAF42210.1; -; Genomic_DNA.
DR   PIR; B81033; B81033.
DR   RefSeq; NP_274872.1; NC_003112.2.
DR   RefSeq; WP_002217983.1; NC_003112.2.
DR   AlphaFoldDB; Q9JXU9; -.
DR   SMR; Q9JXU9; -.
DR   STRING; 122586.NMB1876; -.
DR   PaxDb; Q9JXU9; -.
DR   EnsemblBacteria; AAF42210; AAF42210; NMB1876.
DR   KEGG; nme:NMB1876; -.
DR   PATRIC; fig|122586.8.peg.2397; -.
DR   HOGENOM; CLU_024773_0_0_4; -.
DR   OMA; KRKYNWD; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000425; 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..436
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_0000186795"
FT   DOMAIN          287..436
FT                   /note="N-acetyltransferase"
SQ   SEQUENCE   436 AA;  47299 MW;  1D3854A524544050 CRC64;
     MSAPDLFVAH FREAVPYIRQ MRGKTLVAGI DDRLLEGDTL NKLAADIGLL SQLGIRLVLI
     HGARHFLDRH AAAQGRTPHY CRGLRVTDET SLEQAQQFAG TVRSRFEAAL CGSVSGFARA
     PSVPLVSGNF LTARPIGVID GTDMEYAGVI RKTDTAALRF QLDAGNIVWL PPLGHSYSGK
     TFYLDMLQTA ASAAVSLQAE KLVYLTLSDG ISRPDGTLAE TLSAQEAQSL AEHAGGETRR
     LISSAVAALE GGVHRVQILN GAADGSLLQE LFTRNGIGTS IAKEAFVSIR QAHSGDIPHI
     AALIRPLEEQ GILLHRSREY LENHISEFSI LEHDGNLYGC AALKTFAEAD CGEIACLAVS
     PQAQDGGYGE RLLAHIIDKA RGIGISRLFA LSTNTGEWFA ERGFQTASED ELPETRRKDY
     RSNGRNSHIL VRRLHR