ID ARGA_BUCAI Reviewed; 442 AA.
AC O66143;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 133.
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=BU456;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-71.
RX PubMed=9569646; DOI=10.1016/s0965-1748(97)00092-1;
RA Nakabachi A., Ishikawa H.;
RT "Differential display of mRNAs related to amino acid metabolism in the
RT endosymbiotic system of aphids.";
RL Insect Biochem. Mol. Biol. 27:1057-1062(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 -!- 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; BA000003; BAB13154.1; -; Genomic_DNA.
DR EMBL; AB005263; BAA25386.1; -; mRNA.
DR RefSeq; NP_240268.1; NC_002528.1.
DR RefSeq; WP_009874409.1; NC_002528.1.
DR AlphaFoldDB; O66143; -.
DR SMR; O66143; -.
DR STRING; 563178.BUAP5A_449; -.
DR EnsemblBacteria; BAB13154; BAB13154; BAB13154.
DR KEGG; buc:BU456; -.
DR PATRIC; fig|107806.10.peg.466; -.
DR eggNOG; COG0548; Bacteria.
DR eggNOG; COG1246; Bacteria.
DR HOGENOM; CLU_024773_0_0_6; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000001806; 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 CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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 NCBIfam; TIGR01890; N-Ac-Glu-synth; 1.
DR PANTHER; PTHR30602; AMINO-ACID ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR30602:SF12; AMINO-ACID ACETYLTRANSFERASE NAGS1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR PIRSF; PIRSF000423; ArgA; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..442
FT /note="Amino-acid acetyltransferase"
FT /id="PRO_0000186788"
FT DOMAIN 295..442
FT /note="N-acetyltransferase"
SQ SEQUENCE 442 AA; 49226 MW; C7F67E99C285A394 CRC64;
MKERNTELVQ GFRHSVPYIN AHRGKTFVIM LGGEAIKYGN FYSIINDIGL LHSLGIRLVV
VYGACPQINT SLKEKNIKII YHKSIRITDL ASLEQVKQAA GKLQLDITAR LSMSLTNTPL
QGANISVVSG NFIISQPLGV DDGVDYCHSG RVRRIDKNAI NCQLNNGAIV LIGPVAVSVT
GESFNLTSEE IATQVSIELK AEKMIGFCGN QGVINDEGKI ISELLSNDIK NIIKKLEKKG
DYISSTVRFL KGSIKACKSG VNRSHLISYH KSGALLQELF SRDGIGTQMV MESAEKIRGA
SINDIGGILE LIRPLEHKGI LVRRSREQLE IEVDKFTIIE HDNLTIACAA LYPFFKEKIG
EMACLAVHPD YRNSSRGDAL LKKIKMNAKD MHLKRIFVLT TQSIHWFQER GFILVDIEVL
PESKKKMYNY QRGSKILMID VI
//
