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ARGJ_ASHGO
ID   ARGJ_ASHGO              Reviewed;         443 AA.
AC   Q759Y5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03124};
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE              Short=GAT {ECO:0000255|HAMAP-Rule:MF_03124};
DE              EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_03124};
DE     AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE              Short=OATase {ECO:0000255|HAMAP-Rule:MF_03124};
DE     AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_03124};
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE              EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_03124};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_03124};
DE              Short=AGS {ECO:0000255|HAMAP-Rule:MF_03124};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_03124};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_03124};
DE   Flags: Precursor;
GN   OrderedLocusNames=ADR138C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 119.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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:0000255|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:0000255|HAMAP-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:0000255|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:0000255|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:0000255|HAMAP-
CC       Rule:MF_03124}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000255|HAMAP-
CC       Rule:MF_03124}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|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:0000255|HAMAP-
CC       Rule:MF_03124}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       Rule:MF_03124}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_03124}.
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DR   EMBL; AE016817; AAS52058.2; -; Genomic_DNA.
DR   RefSeq; NP_984234.2; NM_209587.2.
DR   AlphaFoldDB; Q759Y5; -.
DR   SMR; Q759Y5; -.
DR   STRING; 33169.AAS52058; -.
DR   MEROPS; T05.001; -.
DR   EnsemblFungi; AAS52058; AAS52058; AGOS_ADR138C.
DR   GeneID; 4620395; -.
DR   KEGG; ago:AGOS_ADR138C; -.
DR   eggNOG; KOG2786; Eukaryota.
DR   HOGENOM; CLU_027172_1_0_1; -.
DR   InParanoid; Q759Y5; -.
DR   OMA; DYVHENS; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00111.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central.
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   GO; GO:0006592; P:ornithine biosynthetic process; IBA:GO_Central.
DR   CDD; cd02152; OAT; 1.
DR   Gene3D; 3.10.20.340; -; 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   PANTHER; PTHR23100; PTHR23100; 1.
DR   Pfam; PF01960; ArgJ; 1.
DR   SUPFAM; SSF56266; SSF56266; 1.
DR   TIGRFAMs; TIGR00120; ArgJ; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Autocatalytic cleavage; Mitochondrion; Multifunctional enzyme;
KW   Reference proteome; Transferase.
FT   CHAIN           1..216
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT                   /id="PRO_0000398010"
FT   CHAIN           217..443
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT                   /id="PRO_0000398011"
FT   ACT_SITE        217
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         438
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   SITE            137
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   SITE            138
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   SITE            216..217
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
SQ   SEQUENCE   443 AA;  46684 MW;  D4C1FD97806B9C64 CRC64;
     MKSSLSLCQR AANAASKYER YVPSCGVFPL GFKVGSIATG VKKNGQLDLG VILSTYEREG
     GATAAAVFTT NKFKAAPVVA SKERLAKSEG RGISAIVVNS GCANAVTGAV GLENANKVVQ
     LVEQQLGRKD TTLLMSTGVI GQHLSMDKIE HGLGTLLNND DAFGNDFSSW LSLSKAMMTT
     DTFPKLISSR FTLPGGTTYT LTGISKGAGM ICPNMATLLG FIGTDLPISP SALQNILSSA
     VDRSFNCISV DGDMSTNDTI YMLASGAIDT DLITESSESF PLIKAQVTEL AQNLAQLVVR
     DGEGSTKFVT VHVKRALNFA DAKVIAKTIS NSSLVKCALY GQDANWGRIL CAIGYAQLGD
     CASLDESTLN VSFVGVGDSK GAELNLVVDG VPNVNINESK AATMLADTDL KIVVDLGTGT
     EECNFWTCDL SHEYISINAD YRS
 
 
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