ID A0A0D6PAT9_9PROT Unreviewed; 406 AA. AC A0A0D6PAT9; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 15-FEB-2017, entry version 14. DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {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 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 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; Proteobacteria; 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 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: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L- CC glutamate. {ECO:0000256|HAMAP-Rule:MF_01106}. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L- CC ornithine + N-acetyl-L-glutamate. {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, ECO:0000256|SAAS:SAAS00250247}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106, CC ECO:0000256|SAAS:SAAS00250260}. 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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_BANC01000010.1. DR EnsemblBacteria; GAN78870; GAN78870; Aam_010_048. DR UniPathway; UPA00068; UER00106. DR Proteomes; UP000032668; 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-HAMAP. DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR CDD; cd02152; OAT; 1. DR Gene3D; 3.60.70.12; -; 1. DR HAMAP; MF_01106; ArgJ; 1. DR InterPro; IPR002813; Arg_biosynth_ArgJ. DR InterPro; IPR016117; ArgJ-like_dom. 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 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:UP000032668}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106, KW ECO:0000256|SAAS:SAAS00435592}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106}; KW Reference proteome {ECO:0000313|Proteomes:UP000032668}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01106, KW ECO:0000313|EMBL:GAN78870.1}. FT ACT_SITE 196 196 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 159 159 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 185 185 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 196 196 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 278 278 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 401 401 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 406 406 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT SITE 122 122 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 123 123 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 195 196 Cleavage; by autolysis. FT {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 //