ARGA_SALTY
ID ARGA_SALTY Reviewed; 443 AA.
AC Q8ZMB8;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=STM2992;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 -!- 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; AE006468; AAL21868.1; -; Genomic_DNA.
DR PIR; S12388; S12388.
DR RefSeq; NP_461909.1; NC_003197.2.
DR RefSeq; WP_000588964.1; NC_003197.2.
DR AlphaFoldDB; Q8ZMB8; -.
DR SMR; Q8ZMB8; -.
DR STRING; 99287.STM2992; -.
DR PaxDb; Q8ZMB8; -.
DR EnsemblBacteria; AAL21868; AAL21868; STM2992.
DR GeneID; 1254515; -.
DR KEGG; stm:STM2992; -.
DR PATRIC; fig|99287.12.peg.3166; -.
DR HOGENOM; CLU_024773_0_0_6; -.
DR OMA; KRKYNWD; -.
DR PhylomeDB; Q8ZMB8; -.
DR BioCyc; SENT99287:STM2992-MON; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000001014; 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_0000186805"
FT DOMAIN 296..443
FT /note="N-acetyltransferase"
SQ SEQUENCE 443 AA; 49278 MW; 7400B522E653EAD9 CRC64;
MIKERKTELV EGFRHSVPYI NTHRGKTFVI MLGGEAIEHD NFSSIVSDIG LLHSLGIRLV
VVYGARPQID ANLAAHHHEP IYHKNTRVTD AKALELVKQA AGLLQLDITA RLSMSLNNTP
LQGAHINVVS GNFTIAQPLG VDDGVDYCHS GRIRRIDEDA INRQLDNGAI VLMGPVAVSV
TGESFNLTSE EIATQLAVKL KAEKMIGFCS SQGVTNSEGG IISELFPNEA QARVEELEAQ
GDYNSGTVRF LRGAVKACRS GVRRCHLISY QEDGSLLQEL FSRDGIGTQI VMESAEQIRR
ATINDIGGIL ELIRPLEQQG ILVRRSREQL EMEIDKFTII QRDNMTIACA ALYPFVEEKI
GEMACVAVHP DYRSSSRGEV LLERVAAQAR QMGLRKLFVL TTRSIHWFQE RGFTPVDIEL
LPESKKKMYN YQRRSKVLMA DLG