ID G4QFK7_GLANF Unreviewed; 439 AA.
AC G4QFK7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01105};
DE EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_01105};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_01105};
DE Short=AGS {ECO:0000256|HAMAP-Rule:MF_01105};
DE Short=NAGS {ECO:0000256|HAMAP-Rule:MF_01105};
GN Name=argA {ECO:0000256|HAMAP-Rule:MF_01105,
GN ECO:0000313|EMBL:AEP28632.1};
GN OrderedLocusNames=GNIT_0478 {ECO:0000313|EMBL:AEP28632.1};
OS Glaciecola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP28632.1, ECO:0000313|Proteomes:UP000009282};
RN [1] {ECO:0000313|EMBL:AEP28632.1, ECO:0000313|Proteomes:UP000009282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12485 / KCTC 12276 / FR1064
RC {ECO:0000313|Proteomes:UP000009282};
RX PubMed=22123761; DOI=10.1128/JB.06296-11;
RA Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Complete genome sequence of seawater bacterium Glaciecola nitratireducens
RT FR1064T.";
RL J. Bacteriol. 193:7006-7007(2011).
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:0000256|ARBA:ARBA00000016, ECO:0000256|HAMAP-
CC Rule:MF_01105};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000256|ARBA:ARBA00004925,
CC ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- MISCELLANEOUS: In bacteria which possess the bifunctional enzyme
CC ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA
CC fulfills an anaplerotic role. {ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC {ECO:0000256|ARBA:ARBA00009145, ECO:0000256|HAMAP-Rule:MF_01105}.
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DR EMBL; CP003060; AEP28632.1; -; Genomic_DNA.
DR RefSeq; WP_014107509.1; NC_016041.1.
DR AlphaFoldDB; G4QFK7; -.
DR STRING; 1085623.GNIT_0478; -.
DR KEGG; gni:GNIT_0478; -.
DR eggNOG; COG0548; Bacteria.
DR eggNOG; COG1246; Bacteria.
DR HOGENOM; CLU_024773_0_0_6; -.
DR OrthoDB; 9802238at2; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000009282; 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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01105};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01105};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_01105}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105};
KW Reference proteome {ECO:0000313|Proteomes:UP000009282};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01105}.
FT DOMAIN 290..438
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 439 AA; 48418 MW; E938F42D06C2D59E CRC64;
MALSDTESIR LFRSSAPYIN AHRGKTFVIM FGGEAIEDPN FPRIIQDIAL LNSLGVRLII
VHGARPQIDL RLQLRNKESM FRDGIRVTNK ETLECVKDAA GSLRSQIEAL LTMGLPNSPM
HGSQIRVCSG NLVVARPLGV RNGVDFENTG LVRRIDVQGI NDHLSDGSIV LLSPMGYSPT
GEVFNLSHED VATQAAIAMK ADKIITLSER DGIFNQDGRL LRTIELNLIK KELALANIDA
ETTCLTAMIA SVEAGVSRAH CINYHTDGAL LKELFTRDGA GSLVLQNHYE QLRTATIDDV
GGILKLIKPL EESGALVKRS RERLENEIDL FTVIVRDGMI IACAALYMYK SDACGELACV
ATHHDYRGGN RGERLLEEIR KKAILSGLER IFVLTTVTAH WFLEQGFAET TVDALPSAKK
EMYNFTRNSK VFMLSLAPN
//
