ID   ARGJ_RHOFA              Reviewed;         403 AA.
AC   P96426; Q93JQ2;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 116.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              Short=OATase {ECO:0000255|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01106};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              Short=AGSase {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_01106};
GN   Name=argJ {ECO:0000255|HAMAP-Rule:MF_01106}; Synonyms=attH;
OS   Rhodococcoides fascians (Rhodococcus fascians).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Nocardiaceae; Rhodococcoides.
OX   NCBI_TaxID=1828;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D188;
RX   PubMed=11004184; DOI=10.1128/jb.182.20.5832-5840.2000;
RA   Temmerman W., Vereecke D., Dreesen R., Van Montagu M., Holsters M.,
RA   Goethals K.;
RT   "Leafy gall formation is controlled by fasR, an AraC-type regulatory gene
RT   in Rhodococcus fascians.";
RL   J. Bacteriol. 182:5832-5840(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D188;
RX   PubMed=11679063; DOI=10.1046/j.1365-2958.2001.02615.x;
RA   Maes T., Vereecke D., Ritsema T., Cornelis K., Thu H.N., Van Montagu M.,
RA   Holsters M., Goethals K.;
RT   "The att locus of Rhodococcus fascians strain D188 is essential for full
RT   virulence on tobacco through the production of an autoregulatory
RT   compound.";
RL   Mol. Microbiol. 42:13-28(2001).
CC   -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC       version of arginine biosynthesis: the synthesis of N-acetylglutamate
CC       from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by
CC       transacetylation between N(2)-acetylornithine and glutamate.
CC       {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(2)-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate +
CC         L-ornithine; 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_01106};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+);
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_01106};
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_01106}.
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_01106}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC43342.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Y09820; CAA70949.1; -; Genomic_DNA.
DR   EMBL; AJ311775; CAC43342.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P96426; -.
DR   SMR; P96426; -.
DR   STRING; 1443905.GCA_000761075_00044; -.
DR   eggNOG; COG1364; Bacteria.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00111.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:L-glutamate N-acetyltransferase activity, acting on acetyl-CoA as donor; IEA:UniProtKB-UniRule.
DR   GO; GO:0004358; F:L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006592; P:L-ornithine biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd02152; OAT; 1.
DR   FunFam; 3.10.20.340:FF:000003; Arginine biosynthesis bifunctional protein ArgJ; 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   NCBIfam; NF003802; PRK05388.1; 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; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Autocatalytic cleavage; Cytoplasm; Multifunctional enzyme; Transferase.
FT   CHAIN           1..193
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT                   /id="PRO_0000002227"
FT   CHAIN           194..403
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT                   /id="PRO_0000002228"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        194
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         403
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   SITE            125
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_01106"
FT   SITE            126
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_01106"
FT   SITE            193..194
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
SQ   SEQUENCE   403 AA;  42800 MW;  B596508AD60FD900 CRC64;
     MVQSVLSSTS HGSERADMSA ASPQGFHCWT THLGLADEGK DDFSMVISDR PCTSSVVFTK
     SLFAGPCVTL SKTSIEQTSP RGVLVLAKNA NVATGAEGLR NASEIRASVA RTVGIEPDAL
     IMASTGVIGV QYPMDTIRAG LDGLGQGTPL DAHAVARAIM TTDTRAKVSE RAVGTSTIVG
     IAKGVGMIEP DMATMLSFVF TDADVPQDTL NRIFRDVVDR TYNSVSIDTD TSTSDTAAVF
     ANGSAGPVPD TEFEQALEEV CTDLVKMIAS DGEGATKLIV TTVSGASSER QARVVGKSII
     NSPLVKTMIH GEDPNWGRVL MAIGKCSNEV DIEPDRIRVA FADIDVYPSS SLDQHDTVEV
     VREHLATVTV EINVDLGIGT DTWRVFGCDL TDEYIRINAD YTT
//