ID A0A0J7K005_LASNI Unreviewed; 447 AA.
AC A0A0J7K005;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=amino-acid N-acetyltransferase {ECO:0000256|ARBA:ARBA00012697};
DE EC=2.3.1.1 {ECO:0000256|ARBA:ARBA00012697};
GN ORFNames=RF55_19112 {ECO:0000313|EMBL:KMQ83778.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ83778.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ83778.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ83778.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) 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};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004925}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC {ECO:0000256|ARBA:ARBA00009145}.
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:KMQ83778.1}.
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DR EMBL; LBMM01018466; KMQ83778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7K005; -.
DR STRING; 67767.A0A0J7K005; -.
DR PaxDb; 67767-A0A0J7K005; -.
DR OrthoDB; 46762at2759; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
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};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 301..440
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 447 AA; 49980 MW; 3A490420E96E5AFB CRC64;
MQRGLPVKER STELVQGFRH SVPYINAHRG KTFVIMLGGE AIEHENFSNI VNDIGLLHSL
GIRLVVVYGA RPQIDANLAQ HNYEPIYHKH TRVTDAHTLE LVKQAAGLLQ LDITARLSMS
LNNTPLQGAH INVVSGNFII AQPLGVDDGI DYCHSGRIRR IDEEAIHRQL DSNAIVLIGP
VAVSVTGESF NLTSEEVATQ LAIKLKAEKM IGFCSSQGVT DAEGNILSEL FPNDAQKRLE
ELEEGGDYHS GTVRFLRGAV KGCRSGVRRS HLISYQEDGA LVQELFSRDG IGTQIVMESA
EQVRRATIND IGGILELIRP LEQQGILVRR SREQLEMEID KFTIIERDNL TIACAALYPF
PEEKIGEMAC VAVHPDYRSS SRGEMLLQRV ENQARQMGLK KLFVLTTRSI HWFQERGFTP
AEVDVLPMQK QALYNYQRRS KILLADL
//