ID A0A7C8AP78_UNCDE Unreviewed; 419 AA. AC A0A7C8AP78; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 13-SEP-2023, entry version 10. 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:HIJ76857.1}; GN ORFNames=HPP81_09110 {ECO:0000313|EMBL:HIJ76857.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:HIJ76857.1, ECO:0000313|Proteomes:UP000587694}; RN [1] {ECO:0000313|EMBL:HIJ76857.1, ECO:0000313|Proteomes:UP000587694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MAG_17929_sntb_26 {ECO:0000313|EMBL:HIJ76857.1}; RX PubMed=32737307; RA Uzun M., Alekseeva L., Krutkina M., Koziaeva V., Grouzdev D.; RT "Unravelling the diversity of magnetotactic bacteria through analysis of RT open genomic databases."; RL Sci. Data 7:252-250(2020). 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 -!- 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:HIJ76857.1}. 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; DUZL01000097; HIJ76857.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7C8AP78; -. DR UniPathway; UPA00068; UER00106. DR Proteomes; UP000587694; 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..202 FT /note="Arginine biosynthesis bifunctional protein ArgJ FT alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5028544385" FT CHAIN 203..419 FT /note="Arginine biosynthesis bifunctional protein ArgJ beta FT chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5028544384" FT ACT_SITE 203 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 165 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 192 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 203 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 290 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 414 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 419 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT SITE 128 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 129 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 202..203 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" SQ SEQUENCE 419 AA; 44089 MW; 9AF08B53A2C952EC CRC64; MTPVPAEAAK NTKNVTVSRG PFEVAGFLAG AVESGMRYSG RLDLALICAQ DPAGCAASGV FTRNFFCAAP VELCRERLEK HRARAILANA GIANACTGGE GKIRAIEMAR IASDALGCPA DSVLVSSTGV IGMQVDLDPV ARCMPRLIHS LRPDGWEDAA RAIMTTDTVE KMASAHVELG ANLSVTVAGI AKGAGMIAPD MATLLVFACT DAAVSPEVLD HWTRSGADSS FNCITVDGDT STNDSLIVLA GGAAGNSPIT DIGSSESRVF GMALASVLRD LALQVVMDAE GATVLIEIEV RGAADRESAR QVAFTVANSP LVKTAFFGRD ANWGRIVAAV GRSGVKLMPE RVCLFFEDLC VFENGAPVLG EQIEQKASRI FKQKQIRVLL DLGLGDGSFT AWTCDFSFDY VKINASYRS //