ID A0A421DFR2_9EURO Unreviewed; 466 AA.
AC A0A421DFR2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 10.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03124};
DE Includes:
DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE Short=GAT {ECO:0000256|HAMAP-Rule:MF_03124};
DE EC=2.3.1.35 {ECO:0000256|HAMAP-Rule:MF_03124};
DE AltName: Full=Ornithine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE Short=OATase {ECO:0000256|HAMAP-Rule:MF_03124};
DE AltName: Full=Ornithine transacetylase {ECO:0000256|HAMAP-Rule:MF_03124};
DE Includes:
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_03124};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_03124};
DE Short=AGS {ECO:0000256|HAMAP-Rule:MF_03124};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000256|HAMAP-Rule:MF_03124};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000256|HAMAP-Rule:MF_03124};
GN ORFNames=CFD26_108378 {ECO:0000313|EMBL:RLM00909.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLM00909.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|EMBL:RLM00909.1, ECO:0000313|Proteomes:UP000215289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLM00909.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC version of arginine biosynthesis: the synthesis of acetylglutamate from
CC glutamate and acetyl-CoA, and of ornithine by transacetylation between
CC acetylornithine and glutamate. {ECO:0000256|HAMAP-Rule:MF_03124}.
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, ECO:0000256|HAMAP-
CC Rule:MF_03124};
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|HAMAP-Rule:MF_03124};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine
CC (cyclic): step 1/1. {ECO:0000256|HAMAP-Rule:MF_03124}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000256|HAMAP-
CC Rule:MF_03124}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000256|HAMAP-
CC Rule:MF_03124}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-
CC Rule:MF_03124}.
CC -!- PTM: The alpha and beta chains are autoproteolytically processed from a
CC single precursor protein within the mitochondrion. {ECO:0000256|HAMAP-
CC Rule:MF_03124}.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|ARBA:ARBA00006774,
CC ECO:0000256|HAMAP-Rule:MF_03124}.
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:RLM00909.1}.
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DR EMBL; NIDN02000010; RLM00909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421DFR2; -.
DR STRING; 1245748.A0A421DFR2; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004358; F: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; 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, ECO:0000256|HAMAP-
KW Rule:MF_03124};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_03124};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_03124};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW Rule:MF_03124};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03124};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_03124}; Reference proteome {ECO:0000313|Proteomes:UP000215289};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03124}.
FT CHAIN 1..233
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT /id="PRO_5023317206"
FT CHAIN 234..466
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT /id="PRO_5023317207"
FT ACT_SITE 234
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT SITE 155
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT SITE 156
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT SITE 233..234
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
SQ SEQUENCE 466 AA; 49065 MW; 671DD8998D15AE47 CRC64;
MVSPAQPAAA MAAFARMVKG QVRNYSAPLD MAIPASKQKY IPSSGSYPKG FLVSGTHVGV
KASNTKFPDL ALISSETPCS AAAVFTTNKF QAAPVQVSKK TLQSRQGQGI RSVVINSGCA
NAVTGKGGLE DAVNMGRKVD ECNGLREPST LVMSTGVIGQ RLPISKILDK IPTAHANLAS
THDAWLTTAR AICTTDTFPK LLSRTFTLPS SPGRTYSLAG MTKGAGMIHP NMATLLGVLC
TDAPIDPSAL HSLLKHAVSR SFNSISVDGD TSTNDTVAIL ANGAAGGAPI SSPASDDYTA
MQDILTSFAQ SLSQLVVRDG EGATKFVTVR VQNSPHYESA RLIASTIARS PLVKTALYGR
DANWGRILCA IGYTQGVAPG TVVPERTSVS FKPVDGSPVL KLLVNGEPEQ VDEERASVIL
QEEDLEIVVD LGGGEKGEQG LGGEEAVYWF CDFSHEYVTI NGDYRT
//
