ARGA_ALIFM
ID ARGA_ALIFM Reviewed; 446 AA.
AC B5FAS8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, 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=VFMJ11_0599;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) 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 -!- 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; CP001139; ACH66226.1; -; Genomic_DNA.
DR RefSeq; WP_012533582.1; NC_011184.1.
DR AlphaFoldDB; B5FAS8; -.
DR SMR; B5FAS8; -.
DR EnsemblBacteria; ACH66226; ACH66226; VFMJ11_0599.
DR KEGG; vfm:VFMJ11_0599; -.
DR HOGENOM; CLU_024773_0_0_6; -.
DR OMA; KRKYNWD; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000001857; Chromosome I.
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..446
FT /note="Amino-acid acetyltransferase"
FT /id="PRO_1000137054"
FT DOMAIN 299..431
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
SQ SEQUENCE 446 AA; 49518 MW; 96BCA559C0F9FD69 CRC64;
MKFRSTALVK GFRQSAPYVN AHRDKTVVIM LGGEAIADPN FANIVNDIAL LNSLGLRIVI
VYGTRPQMRS LLKQTEHHAP FHKGIRITDE QTLELVKQIA GQLQLDITAR LSMSLNNTPM
AGAQINVISG NFVIAQPLGV DDGIDYCHSG RVRRIDTQGI NRMLDQQSIV LLGPVASSVT
GECFNLLSED VATQLAIRLN ADKLIGFCSE QGVLNEKGQI LAELFPSEAE EILQRLEKEL
TPENGKLTGT MRFLKGAISA CKAGVPRSHL ISYKEDGALI QELFSFDGIG TQVVMASSEQ
VRDAEIDDIG GILDLIRPLE EEGILVRRSR EQLEQEIAQF TIIEKDGLVI ACAALYPFPE
EGMAEMGCVA VHPDYRDGDR GVILLNRLRA KAKQYKLSQL FVLTTRSLHW FREQGFIEVD
VSHLPMKKQK LYNFQRKSKI LVLKGL