ARGA_PSEAB
ID ARGA_PSEAB Reviewed; 432 AA.
AC Q02EG0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=PA14_68740;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ14588.1; -; Genomic_DNA.
DR RefSeq; WP_003096265.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02EG0; -.
DR SMR; Q02EG0; -.
DR PRIDE; Q02EG0; -.
DR EnsemblBacteria; ABJ14588; ABJ14588; PA14_68740.
DR KEGG; pau:PA14_68740; -.
DR HOGENOM; CLU_024773_0_0_6; -.
DR OMA; KRKYNWD; -.
DR BioCyc; PAER208963:G1G74-5793-MON; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000000653; 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..432
FT /note="Amino-acid acetyltransferase"
FT /id="PRO_1000084816"
FT DOMAIN 286..425
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
SQ SEQUENCE 432 AA; 47859 MW; 725FAD778FD44A4E CRC64;
MPDYVNWLRH ASPYINSHRD RTFVVMLPGE GVEHPNFGNI VHDLVLLHSL GARLVLVHGS
RPQIEARLAA RGLAPRYHRD LRVTDAPTLE CVIDAVGSLR IAIEARLSMD MAASPMQGAR
LRVAGGNLVT ARPIGVVEGV DYHHTGEVRR IDRKGIGRLL DERSIVLLSP LGYSPTGEIF
NLACEDVAMR AAIDLEAEKL ILYGAEQGLL DASGKLVREL RPQQVPAHLQ RLGNSYQAEL
LDAAAQACRA GVKRSHIVSY TEDGALLSEL FTRTGNGTLV AQEQFEQLRE AGIEDVGGLI
ELIRPLEEQG ILVRRSREVL EREIEQFSIV EREGLIIACA ALYPIADSEA GELACLAVNP
EYRHGGRGDE LLERIEERAR GLGLKTLFVL TTRTAHWFRE RGFQPSSVER LPAARASLYN
FQRNSQVFEK SL