ID A0A2I0FY99_9GAMM Unreviewed; 442 AA.
AC A0A2I0FY99;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=CIG19_06585 {ECO:0000313|EMBL:PKH25044.1};
OS Enterobacterales bacterium CwR94.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales.
OX NCBI_TaxID=2025587 {ECO:0000313|EMBL:PKH25044.1, ECO:0000313|Proteomes:UP000237543};
RN [1] {ECO:0000313|EMBL:PKH25044.1, ECO:0000313|Proteomes:UP000237543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CwR94 {ECO:0000313|EMBL:PKH25044.1,
RC ECO:0000313|Proteomes:UP000237543};
RA de Groot N.N.;
RL Submitted (AUG-2017) 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: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 -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643,
CC ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKH25044.1}.
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DR EMBL; NVXY01000004; PKH25044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0FY99; -.
DR OrthoDB; 9802238at2; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000237543; Unassembled WGS sequence.
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:UP000237543};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01105}.
FT DOMAIN 295..442
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 442 AA; 49233 MW; CC1E6BB463337835 CRC64;
MKERSTELVQ GFRHTVPYIN AHRGKTFVIM LGGEAIEHEN FSSIVNDIGL LHSLGIRLVV
VYGARPQIDA SLAEHQLEPV YHKHIRVTDA QSLELVKQAA GRLQLDITAR LSMSLSNTPL
QGAHINVVSG NFIIAQPLGV DDGVDYCHSG RIRRLDEEAI HRQLDSGAIV LLGPVAVSVT
GESFNLTSEE VATQVAIKLR AEKMLGFCSE QGVTTAEGNI ISELFPGEAL EKINELEAAG
DYHSGTVRFL RGAVKACRSG VRRSHLMSYQ SDGALLQELF SRDGIGTQIV MESAEQIRRA
TINDIGGILE LIRPLEQQGI LVRRSREQLE IEIDKFTIIE RDNLTIACAA LYPFPEEKIG
EMACVAVHPE YRSSSRGEEL LNRVALQAKQ MGLEKLFVLT TRSIHWFQER GFTPVDIELL
PESKKEMYNY QRRSKVLMAD LR
//
