ID A0A0D6PAT9_9PROT Unreviewed; 406 AA. AC A0A0D6PAT9; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 27-NOV-2024, entry version 42. DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000256|HAMAP-Rule:MF_01106}; DE Includes: DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106}; DE EC=2.3.1.35 {ECO:0000256|HAMAP-Rule:MF_01106}; DE AltName: Full=Ornithine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106}; DE Short=OATase {ECO:0000256|HAMAP-Rule:MF_01106}; DE AltName: Full=Ornithine transacetylase {ECO:0000256|HAMAP-Rule:MF_01106}; DE Includes: DE RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106}; DE EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_01106}; DE AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_01106}; DE Short=AGSase {ECO:0000256|HAMAP-Rule:MF_01106}; DE Contains: DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000256|HAMAP-Rule:MF_01106}; DE Contains: DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000256|HAMAP-Rule:MF_01106}; GN Name=argJ {ECO:0000256|HAMAP-Rule:MF_01106}; GN ORFNames=Aam_010_048 {ECO:0000313|EMBL:GAN78870.1}; OS Acidocella aminolytica 101 = DSM 11237. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidocella. OX NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN78870.1, ECO:0000313|Proteomes:UP000032668}; RN [1] {ECO:0000313|EMBL:GAN78870.1, ECO:0000313|Proteomes:UP000032668} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668}; RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.; RT "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237."; RL Submitted (NOV-2012) 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 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:0000256|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:0000256|ARBA:ARBA00000498, ECO:0000256|HAMAP- CC 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:0000256|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:0000256|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:0000256|HAMAP- CC Rule:MF_01106}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. CC {ECO:0000256|ARBA:ARBA00011475, ECO:0000256|HAMAP-Rule:MF_01106}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106}. CC -!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e., CC capable of catalyzing only the fifth step of the arginine biosynthetic CC pathway. {ECO:0000256|HAMAP-Rule:MF_01106}. CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|ARBA:ARBA00006774, CC ECO:0000256|HAMAP-Rule:MF_01106}. 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:GAN78870.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BANC01000010; GAN78870.1; -; Genomic_DNA. DR RefSeq; WP_048877354.1; NZ_FQVJ01000020.1. DR AlphaFoldDB; A0A0D6PAT9; -. DR STRING; 1120923.SAMN02746095_02318; -. DR OrthoDB; 9804242at2; -. DR UniPathway; UPA00068; UER00106. DR Proteomes; UP000032668; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004042; F:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006592; P: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 FunFam; 3.60.70.12:FF:000001; Arginine biosynthesis bifunctional protein ArgJ, chloroplastic; 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_01106}; Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106}; KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP- KW Rule:MF_01106}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106}; KW Reference proteome {ECO:0000313|Proteomes:UP000032668}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01106}. FT CHAIN 1..195 FT /note="Arginine biosynthesis bifunctional protein ArgJ FT alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5023396363" FT CHAIN 196..406 FT /note="Arginine biosynthesis bifunctional protein ArgJ beta FT chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5023396364" FT ACT_SITE 196 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 159 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 185 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 196 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 278 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 401 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 406 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT SITE 122 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_01106" FT SITE 123 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_01106" FT SITE 195..196 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" SQ SEQUENCE 406 AA; 41713 MW; FCEDED7AC36D3882 CRC64; MAGQLPVSPL ALPMPELPPI AGVRLATAEA GIRYKGRTDV LLAELAAGTA VAGVFTRNLC PGAPVTWCRQ VLPGGLARGL VVNAGNANVF NGAVGVRAVE TTAQAAATTL GTAPEQIFLA STGVIGEPLP AERIVAVMDG LKASLKQDRF AEAAKAIMTT DTFPKGATRT VELGGKTVRI NGIAKGSGMI APDMATMLCF IFTDAAIPAS ALQDMLAGGV ERTFNCVTID SDTSTSDTVL LFATGQAGND LNADLTGFRE ALHQVLHELA LLVVRDGEGA QKFVTINVQG AVSDASAKKI GLAIANSPLV KTAIAGEDAN WGRIVMAVGK AGEPADRDTL GVAVGGVWMA RAGGVVPGYD EAPVVAHMKG RKIEITVDIG LGEGKATVWT CDLTHGYIDI NGSYRS //