ID A0A3A6NM02_9BACT Unreviewed; 398 AA. AC A0A3A6NM02; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 27-NOV-2024, entry version 19. 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:RJX25911.1}; GN ORFNames=C4531_16695 {ECO:0000313|EMBL:RJX25911.1}; OS Desulfurivibrio sp. OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales; OC Desulfobulbaceae; Desulfurivibrio. OX NCBI_TaxID=2093369 {ECO:0000313|EMBL:RJX25911.1, ECO:0000313|Proteomes:UP000284985}; RN [1] {ECO:0000313|EMBL:RJX25911.1, ECO:0000313|Proteomes:UP000284985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SURF_16 {ECO:0000313|EMBL:RJX25911.1}; RX PubMed=28644444; DOI=10.1038/ismej.2017.94; RA Momper L., Jungbluth S.P., Lee M.D., Amend J.P.; RT "Energy and carbon metabolisms in a deep terrestrial subsurface fluid RT microbial community."; RL ISME J. 11:2319-2333(2017). 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:RJX25911.1}. 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; QZKJ01000109; RJX25911.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3A6NM02; -. DR UniPathway; UPA00068; UER00106. DR Proteomes; UP000284985; 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:000001; Arginine biosynthesis bifunctional protein ArgJ, chloroplastic; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01106}. FT CHAIN 1..182 FT /note="Arginine biosynthesis bifunctional protein ArgJ FT alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5023391205" FT CHAIN 183..398 FT /note="Arginine biosynthesis bifunctional protein ArgJ beta FT chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5023391206" FT ACT_SITE 183 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 146 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 172 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 183 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 393 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 398 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT SITE 109 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 110 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 182..183 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" SQ SEQUENCE 398 AA; 41663 MW; 3F57810A30E0395A CRC64; MNKTLTVPGF KAAAVKAGIR GKDRLDVALI YSETPAAAAG VFTTSKVKAA PVLLDMEYLR DGRAQAIIVN SGIANACTGQ AGMELARGTA RLAAGQLGIA GELVLVASTG VIGQQLDLAI FENCMAPLAG SLRQDGFADV ARAMMTTDTV PKTARRVVEL AGKKITLLGL AKGSGMIMPN MATMLSFIVT DAAVQHEVLQ EMLRQSVAHS FNAVTVDGDT STNDTVLLLA NGQAGNAAIE RLDSADAACF RQALDELCLD LALQIVKDGE GATKLITVQV KGAASVAEAD QAARTVANSS LVKTAFFGED ANWGRIIAAL GRAGIDFDPD LVDISFDEVL MVRDGLGLGA EQEKLATRIL KQQAFAVVID LKAGPAEATV YTCDLSVDYI RINADYRS //