ARGA_ECOLI
ID ARGA_ECOLI Reviewed; 443 AA.
AC P0A6C5; O68009; O68010; O68011; O68012; O68013; P08205; Q2MA19;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=b2818, JW2786;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3320971; DOI=10.1093/nar/15.24.10586;
RA Brown K., Finch P.W., Hickson I.D., Emmerson P.T.;
RT "Complete nucleotide sequence of the Escherichia coli argA gene.";
RL Nucleic Acids Res. 15:10586-10586(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF HIS-15; TYR-19;
RP SER-54; ARG-58; GLY-287 AND GLN-432.
RC STRAIN=K12 / Various isolates;
RX PubMed=9572954; DOI=10.1128/aem.64.5.1805-1811.1998;
RA Rajagopal B.S., Deponte J. III, Tuchman M., Malamy M.H.;
RT "Use of inducible feedback-resistant N-acetylglutamate synthetase (argA)
RT genes for enhanced arginine biosynthesis by genetically engineered
RT Escherichia coli K-12 strains.";
RL Appl. Environ. Microbiol. 64:1805-1811(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=K12;
RX PubMed=16890; DOI=10.1016/s0021-9258(17)40387-5;
RA Marvil D.K., Leisinger T.;
RT "N-acetylglutamate synthase of Escherichia coli: purification,
RT characterization, and molecular properties.";
RL J. Biol. Chem. 252:3295-3303(1977).
RN [6]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
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:0000269|PubMed:16890};
CC -!- ACTIVITY REGULATION: Feedback inhibition by L-arginine.
CC {ECO:0000269|PubMed:16890}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000269|PubMed:16890}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000305|PubMed:16890}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16890}.
CC -!- MISCELLANEOUS: The mutant strains shown below are all feedback-
CC resistant (fbr) strains exhibiting enhanced arginine biosynthesis.
CC {ECO:0000305|PubMed:9572954}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC {ECO:0000305}.
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DR EMBL; Y00492; CAA68547.1; -; Genomic_DNA.
DR EMBL; AF008115; AAC23443.1; -; Genomic_DNA.
DR EMBL; AF008116; AAC23444.1; -; Genomic_DNA.
DR EMBL; AF008117; AAC23445.1; -; Genomic_DNA.
DR EMBL; AF008118; AAC23446.1; -; Genomic_DNA.
DR EMBL; AF008119; AAC23447.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40465.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75857.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76887.1; -; Genomic_DNA.
DR PIR; A30372; XYECAA.
DR RefSeq; NP_417295.1; NC_000913.3.
DR RefSeq; WP_000237947.1; NZ_SSUV01000026.1.
DR AlphaFoldDB; P0A6C5; -.
DR SMR; P0A6C5; -.
DR BioGRID; 4262306; 14.
DR DIP; DIP-48037N; -.
DR IntAct; P0A6C5; 3.
DR STRING; 511145.b2818; -.
DR PaxDb; P0A6C5; -.
DR PRIDE; P0A6C5; -.
DR EnsemblBacteria; AAC75857; AAC75857; b2818.
DR EnsemblBacteria; BAE76887; BAE76887; BAE76887.
DR GeneID; 947289; -.
DR KEGG; ecj:JW2786; -.
DR KEGG; eco:b2818; -.
DR PATRIC; fig|1411691.4.peg.3918; -.
DR EchoBASE; EB0061; -.
DR eggNOG; COG0548; Bacteria.
DR eggNOG; COG1246; Bacteria.
DR HOGENOM; CLU_024773_0_0_6; -.
DR InParanoid; P0A6C5; -.
DR OMA; KRKYNWD; -.
DR PhylomeDB; P0A6C5; -.
DR BioCyc; EcoCyc:N-ACETYLTRANSFER-MON; -.
DR BioCyc; MetaCyc:N-ACETYLTRANSFER-MON; -.
DR BRENDA; 2.3.1.1; 2026.
DR SABIO-RK; P0A6C5; -.
DR UniPathway; UPA00068; UER00106.
DR PRO; PR:P0A6C5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0004358; F:glutamate N-acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..443
FT /note="Amino-acid acetyltransferase"
FT /id="PRO_0000186790"
FT DOMAIN 296..443
FT /note="N-acetyltransferase"
FT MUTAGEN 15
FT /note="H->Y: In EE17."
FT /evidence="ECO:0000269|PubMed:9572954"
FT MUTAGEN 19
FT /note="Y->C: In EE51."
FT /evidence="ECO:0000269|PubMed:9572954"
FT MUTAGEN 54
FT /note="S->N: In PT2M217."
FT /evidence="ECO:0000269|PubMed:9572954"
FT MUTAGEN 58
FT /note="R->H: In EE11."
FT /evidence="ECO:0000269|PubMed:9572954"
FT MUTAGEN 287
FT /note="G->S: In PT2M216."
FT /evidence="ECO:0000269|PubMed:9572954"
FT MUTAGEN 432
FT /note="Q->R: In PT2M217."
FT /evidence="ECO:0000269|PubMed:9572954"
SQ SEQUENCE 443 AA; 49195 MW; AE0D84902456797A CRC64;
MVKERKTELV EGFRHSVPYI NTHRGKTFVI MLGGEAIEHE NFSSIVNDIG LLHSLGIRLV
VVYGARPQID ANLAAHHHEP LYHKNIRVTD AKTLELVKQA AGTLQLDITA RLSMSLNNTP
LQGAHINVVS GNFIIAQPLG VDDGVDYCHS GRIRRIDEDA IHRQLDSGAI 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
