ARGA_VIBVY
ID ARGA_VIBVY Reviewed; 445 AA.
AC Q7MIA6;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 110.
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=VV2611;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC95375.1; -; Genomic_DNA.
DR RefSeq; WP_011079707.1; NC_005139.1.
DR AlphaFoldDB; Q7MIA6; -.
DR SMR; Q7MIA6; -.
DR STRING; 672.VV93_v1c23260; -.
DR EnsemblBacteria; BAC95375; BAC95375; BAC95375.
DR KEGG; vvy:VV2611; -.
DR PATRIC; fig|196600.6.peg.2613; -.
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; UP000002675; 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 Reference proteome; Transferase.
FT CHAIN 1..445
FT /note="Amino-acid acetyltransferase"
FT /id="PRO_0000186811"
FT DOMAIN 299..438
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
SQ SEQUENCE 445 AA; 49033 MW; AA9638D7FC647E2B CRC64;
MKIRSTALVK GFRQSTPYVN AHRGKTMVIL LGGEAIADKN FSNIINDIAL MHSLGVKVVL
VYGARPQINQ LLDKQSSQTP YHKHIRVTDE NSLSIVMQAA GQLQLAITAS LSMSLNNTPM
AGTHLNVVSG NFVIAQPLGI DEGVDYCHSG RIRRIDTEAI NRSLDQGSIV LLGPIASSVT
GECFNLLSEE VATQVAIKLK ADKLIGFCSE QGVIDEEGNA VAELFPSDAE KFIQKLSVDV
DPDSDFHSGT LRFLKGAVAA CRAGVPRSHL ISYKIDGALI QELFSFDGIG TQVVMASAEQ
VRQACIDDIG GILELIRPLE EQGILVRRSR EQLEQEVERF TIIEKDGLII GCAALYPYID
EHMAEMACVA IHPDYRDGNR GLLLLNYMKH RSKSIGIEQI FVLTTHSVHW FREQGFYEIG
VDSLPMAKKS LYNYQRRSKI LALPL