ID A0A1G9J370_STREI Unreviewed; 397 AA. AC A0A1G9J370; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 13-NOV-2019, entry version 16. 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; Firmicutes; 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 RT strain 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 CC cyclic version of arginine biosynthesis: the synthesis of N- CC acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, CC and of ornithine by transacetylation between N(2)-acetylornithine CC and glutamate. {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; CC EC=2.3.1.35; Evidence={ECO:0000256|HAMAP-Rule:MF_01106}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L- CC glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288; EC=2.3.1.1; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01106}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)- CC acetyl-L-ornithine (cyclic): step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01106}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-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|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 CC biosynthetic pathway. {ECO:0000256|HAMAP-Rule:MF_01106}. CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|HAMAP- CC 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 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; -; 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 {ECO:0000256|HAMAP-Rule:MF_01106, KW ECO:0000313|EMBL:TFH44758.1}; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106}; KW Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_01106}; KW Complete proteome {ECO:0000313|Proteomes:UP000183162, KW ECO:0000313|Proteomes:UP000298141}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01106, KW ECO:0000313|EMBL:SDL31762.1}. FT ACT_SITE 184 184 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 147 147 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 173 173 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 184 184 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 270 270 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 392 392 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 397 397 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT SITE 113 113 Involved in the stabilization of negative FT charge on the oxyanion by the formation FT of the oxyanion hole. {ECO:0000256|HAMAP- FT Rule:MF_01106}. FT SITE 114 114 Involved in the stabilization of negative FT charge on the oxyanion by the formation FT of the oxyanion hole. {ECO:0000256|HAMAP- FT Rule:MF_01106}. FT SITE 183 184 Cleavage; by autolysis. FT {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 //