ID A0A1G9J370_STREI Unreviewed; 397 AA. AC A0A1G9J370; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 24-JAN-2024, entry version 27. 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 ECO:0000313|EMBL:TFH44758.1}; GN ORFNames=E3305_00680 {ECO:0000313|EMBL:TFH44758.1}, SAMN05216400_0433 GN {ECO:0000313|EMBL:SDL31762.1}; OS Streptococcus equinus (Streptococcus bovis). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1335 {ECO:0000313|EMBL:SDL31762.1, ECO:0000313|Proteomes:UP000183162}; RN [1] {ECO:0000313|EMBL:SDL31762.1, ECO:0000313|Proteomes:UP000183162} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sb09 {ECO:0000313|EMBL:SDL31762.1, RC ECO:0000313|Proteomes:UP000183162}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:TFH44758.1, ECO:0000313|Proteomes:UP000298141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FMD1 {ECO:0000313|EMBL:TFH44758.1, RC ECO:0000313|Proteomes:UP000298141}; RA Zhao W., Yu D., Luo Y.; RT "Identification and pathogenicity analysis of Streptococcus equinus strain RT isolated from forest musk deer with suppurative pneumonia."; RL Submitted (MAR-2019) 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=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_01106}; 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_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 --------------------------------------------------------------------------- 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; FNGX01000001; SDL31762.1; -; Genomic_DNA. DR EMBL; SPDR01000001; TFH44758.1; -; Genomic_DNA. DR RefSeq; WP_021141943.1; NZ_SPDR01000001.1. DR AlphaFoldDB; A0A1G9J370; -. DR OrthoDB; 9804242at2; -. DR UniPathway; UPA00068; UER00106. DR Proteomes; UP000183162; Unassembled WGS sequence. DR Proteomes; UP000298141; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; 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; 3.10.20.340; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01106}. FT CHAIN 1..183 FT /note="Arginine biosynthesis bifunctional protein ArgJ FT alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5025750773" FT CHAIN 184..397 FT /note="Arginine biosynthesis bifunctional protein ArgJ beta FT chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5025750774" FT ACT_SITE 184 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 147 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 173 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 184 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 270 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 392 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 397 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT SITE 113 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 114 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 183..184 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" SQ SEQUENCE 397 AA; 42441 MW; 0B8CEFAA5A65F493 CRC64; MKVIKGNVAS PLGFSADGLH AGFKKRKLDF GWIVSEVPAS VAGVYTTNKV IAAPLIVTRQ SVKKAQKMKA IVVNSGVANS CTGVQGMEDA YTMQKWTAEK LGVEPDLVGV ASTGVIGDLL PMDTLKTGLS KLVVNGNSDD FSKAILTTDT MVKTVAVTEK FGRDEVTMAG VAKGSGMIHP NMATMLAFIT CDANISSETL QLALSQNVET TFNQITVDGD TSTNDMVLVM SNGCTLNEEI LPNTPEFDKF SSMLNYVMQE LAKMIAKDGE GASKLIEVNV KNAPNALDAR MMAKSVVGSS LVKTAIFGED PNWGRILAAV GYAGVDVPVD NIDIFLGDVP VMLKSSPVDF EAEEMQDVMH EDEITITVDL HAGEAQGKAW GCDLSYDYVK INALYRT //