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Database: UniProt
Entry: A0A059LGU6_9CHLO
LinkDB: A0A059LGU6_9CHLO
Original site: A0A059LGU6_9CHLO 
ID   A0A059LGU6_9CHLO        Unreviewed;       397 AA.
AC   A0A059LGU6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=glutamate N-acetyltransferase {ECO:0000256|ARBA:ARBA00013264};
DE            EC=2.3.1.35 {ECO:0000256|ARBA:ARBA00013264};
DE   Flags: Fragment;
GN   ORFNames=H632_c2404p0 {ECO:0000313|EMBL:KDD73229.1};
OS   Helicosporidium sp. ATCC 50920.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Helicosporidium.
OX   NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD73229.1, ECO:0000313|Proteomes:UP000026042};
RN   [1] {ECO:0000313|EMBL:KDD73229.1, ECO:0000313|Proteomes:UP000026042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD73229.1,
RC   ECO:0000313|Proteomes:UP000026042};
RX   PubMed=24809511;
RA   Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT   "A lack of parasitic reduction in the obligate parasitic green alga
RT   helicosporidium.";
RL   PLoS Genet. 10:E1004355-E1004355(2014).
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:KDD73229.1}.
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DR   EMBL; AYPS01002404; KDD73229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059LGU6; -.
DR   STRING; 1291522.A0A059LGU6; -.
DR   OrthoDB; 45829at2759; -.
DR   Proteomes; UP000026042; Unassembled WGS sequence.
DR   GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd02152; OAT; 1.
DR   Gene3D; 3.10.20.340; ArgJ beta chain, C-terminal domain; 1.
DR   Gene3D; 3.60.70.12; L-amino peptidase D-ALA esterase/amidase; 1.
DR   HAMAP; MF_01106; ArgJ; 1.
DR   InterPro; IPR002813; Arg_biosynth_ArgJ.
DR   InterPro; IPR016117; ArgJ-like_dom_sf.
DR   InterPro; IPR042195; ArgJ_beta_C.
DR   NCBIfam; TIGR00120; ArgJ; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000026042};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KDD73229.1"
SQ   SEQUENCE   397 AA;  40740 MW;  5FD8182A3FA19D2A CRC64;
     QGMYAELRLS GEGKADLGLV LSDRPANGAG TFTTNVMCAA PVSWCKRVLS LGRPVRALLV
     NSGQANAATG SLGDENARAS ASGAAVALGL DPDAVLLQST GVIGKQVRME QLLAALPTLA
     KGLERSEEAG RRLAVAMTTT DLAYKSAALE VRLPESGRTV RLGGAAKGSG MIHPNMATML
     GVVTCDAAVD PAVWQVLVSR ATDASYNQIT VDGDTSTNDC VLALCNGAAV GDGHEIKSLE
     SADARALGDA LTALCQGLAK SIAWDGEGAT MLLECQVSGA GNDSDARRVA KSVVGSSLVK
     AAMFGCYPNW GRLAAAAGYA GVSYLQESVA IRLGDIALMR DGQPLEFDFE AARAYLRGVA
     DAHGTAHVHI SIGTGPGKGK AWGCDLSYDY VKINVGA
//
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