ID   ARGA_PECCP              Reviewed;         441 AA.
AC   C6DAG1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=PC1_0919;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001657; ACT11969.1; -; Genomic_DNA.
DR   RefSeq; WP_012773609.1; NC_012917.1.
DR   AlphaFoldDB; C6DAG1; -.
DR   SMR; C6DAG1; -.
DR   STRING; 561230.PC1_0919; -.
DR   EnsemblBacteria; ACT11969; ACT11969; PC1_0919.
DR   KEGG; pct:PC1_0919; -.
DR   eggNOG; COG0548; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   OMA; KRKYNWD; -.
DR   OrthoDB; 901370at2; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000002736; 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   Transferase.
FT   CHAIN           1..441
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_1000213559"
FT   DOMAIN          295..434
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
SQ   SEQUENCE   441 AA;  49078 MW;  CBBC4C70ECA7B47E CRC64;
     MKERSTELVQ GFRHSVPYIN AHRGKTFVIM LGGEAIEHAN FSSIVNDIGL LHSLGIKLVV
     VYGARPQIDA NLTTHHYEPH YHKNTRITDS TTLELVKQAA GMLQLDITAR LSMSLNNTPL
     QGAHINVVSG NFIIAQPLGV DDGVDYCHSG RIRRIDEEAV HRQLNSGAIV LLGPVAVSVT
     GESFNLTSEE VATQLAIKLK AEKMIGFCSS QGVTNEEGSI ISELFPDDAQ RRIDTLEQAG
     DYHSGTVRFL RGAVKACRSG VRRSHLISYQ DDGALLQELF SRDGIGTQIV MESAEQVRRA
     TINDIGGILE LIRPLEEQGI LVRRSREQLE MEIDKFTVVV RDNLTIACAA LYPFPEESIG
     EMACVAVHPD YRSSSRGDML LMRIAAQARQ QGLQKLFVLT THSIHWFQER GFLPAEVEML
     PKKKQALYNY QRRSKILVLD L