ARGA_SALAR
ID ARGA_SALAR Reviewed; 443 AA.
AC A9MS91;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=SARI_04668;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX24435.1; -; Genomic_DNA.
DR RefSeq; WP_000588972.1; NC_010067.1.
DR AlphaFoldDB; A9MS91; -.
DR SMR; A9MS91; -.
DR STRING; 41514.SARI_04668; -.
DR EnsemblBacteria; ABX24435; ABX24435; SARI_04668.
DR KEGG; ses:SARI_04668; -.
DR HOGENOM; CLU_024773_0_0_6; -.
DR OMA; KRKYNWD; -.
DR OrthoDB; 901370at2; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000002084; 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_1000084822"
FT DOMAIN 296..436
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
SQ SEQUENCE 443 AA; 49358 MW; 24E15E72B0FF1FB8 CRC64;
MIKERRTELV EGFRHSVPYI NTHRGKTFVI MLGGEAIEHD NFSSIVNDIG LLHSLGIRLV
VVYGARPQID ANLAAHHHEP IYHKNTRVTD AKTLELVKQA AGLLQLDITA RLSMSLNNTP
LQGAHINVVS GNFTIAQPLG VDDGVDYCHS GRIRRIDEDA INRQLDNGAI VLIGPVAVSV
TGESFNLTSE EIATQLAVKL KAEKMIGFCS SQGVTNSKGD VISELFPNEA QARVEELEAQ
GDYNSGTVRF LRGAVKACRS GVRRCHLISY QEDGTLLQEL FSREGIGTQI VMESAEQIRR
ATINDIGGIL ELIRPLEQQG ILVRRSREQL EMEIDKFTII QRDNMTIACA ALYPFVEEKI
GEMACVAVHP DYRSSSRGEI LLERIAAQAR QMGLSKLFVL TTRSIHWFQE RGFTPVDIEL
LPESKKKMYN YQRRSKVLIA DLG