ID A0A3E2HRC2_SCYLI Unreviewed; 474 AA.
AC A0A3E2HRC2;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 13-SEP-2023, entry version 20.
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=B7463_g466 {ECO:0000313|EMBL:RFU35896.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU35896.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU35896.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU35896.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RFU35896.1}.
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DR EMBL; NCSJ02000004; RFU35896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HRC2; -.
DR STRING; 5539.A0A3E2HRC2; -.
DR OMA; DYVHENS; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; 3.30.2330.10; arginine biosynthesis bifunctional protein suprefamily; 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:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU35896.1"
FT NON_TER 474
FT /evidence="ECO:0000313|EMBL:RFU35896.1"
SQ SEQUENCE 474 AA; 50234 MW; 4AB91D9AF24CF462 CRC64;
MVLRGLQWPA FTDLGRSRAS QCFQGGVRYY SVSLGVTIPA AKQKYVPMGG VYPKGFLVSG
IHVGVKPTNK STPDLAFVTS KIPCAAAAVF TKNKFQAAPV TVSREMLKKR NNDGIRAVIV
NSGCANAVTG KGGIEDAEKM GATADSCLDS ASDNDGGRTI VMSTGVIGQR LPIQKILNKI
PLAYDALGAS HDHWLTAAQA ICTTDTFPKL LSRTFSLPSS PSIEYRIAGM TKGAGMIHPN
MATLLGIIAT DAPIAPGILP SLLTSAVDKS FNSISIDGDT STNDTVAVLA NGAAGGQEIT
SQSSRDYAAF QSTLTEFATD LAKLVVRDGE GATKFVTIRV TDASSEVAAR KIASTIARSP
LVKTALYGKD ANWGRILCAT GYSLISEPGM PISNVQEIVP ERTSVSFIPS NGTPELKLLI
NGEPENIDEA RAAEILEAED LEILVRLGTG KEEAVYWTCD YSHEYITING DYRT
//
