ID A0A2J6MF69_LACSA Unreviewed; 167 AA.
AC A0A2J6MF69;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=glutamate N-acetyltransferase {ECO:0000256|ARBA:ARBA00013264};
DE EC=2.3.1.35 {ECO:0000256|ARBA:ARBA00013264};
GN ORFNames=LSAT_1X104560 {ECO:0000313|EMBL:PLY98175.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY98175.1};
RN [1] {ECO:0000313|EMBL:PLY98175.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-
CC acetyl-L-glutamate; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=2.3.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00000498};
CC -!- SIMILARITY: Belongs to the ArgJ family.
CC {ECO:0000256|ARBA:ARBA00006774}.
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:PLY98175.1}.
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DR EMBL; NBSK01000236; PLY98175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6MF69; -.
DR STRING; 4236.A0A2J6MF69; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_1X104560_mrna; cds-PLY98175.1; gene-LSAT_1X104560.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_1X104560_mrna; cds-PLY98175.1; gene-LSAT_1X104560.
DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.340; ArgJ beta chain, C-terminal domain; 1.
DR InterPro; IPR002813; Arg_biosynth_ArgJ.
DR InterPro; IPR016117; ArgJ-like_dom_sf.
DR InterPro; IPR042195; ArgJ_beta_C.
DR PANTHER; PTHR23100; ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ; 1.
DR PANTHER; PTHR23100:SF0; ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ, MITOCHONDRIAL; 1.
DR Pfam; PF01960; ArgJ; 1.
DR SUPFAM; SSF56266; DmpA/ArgJ-like; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 167 AA; 18129 MW; 6AE0D9C0EB9C912A CRC64;
MRECSRAAAS NYLKEAGDAH GTVKIQISIG DGPGTGLAWG CDLSYDYVKI NYATSLGPGS
LDKCWSSKCS HGYQDVIDCS YALSNPILVY MSKVDGRFNF SPISVNFLTE VAKVIFALVM
LLIHARNQKI GEKPLLSVSS FVQAARNNVL LEIYYKNSTG GSELSTN
//
