ID A0A553Y3J7_9GAMM Unreviewed; 407 AA. AC A0A553Y3J7; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 22-FEB-2023, entry version 9. 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:TSB23791.1}; GN ORFNames=FOR85_04780 {ECO:0000313|EMBL:TSB23791.1}; OS Psychrobacter sp. YGAH215. OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Psychrobacter. OX NCBI_TaxID=2596826 {ECO:0000313|EMBL:TSB23791.1, ECO:0000313|Proteomes:UP000317041}; RN [1] {ECO:0000313|EMBL:TSB23791.1, ECO:0000313|Proteomes:UP000317041} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YGAH215 {ECO:0000313|EMBL:TSB23791.1, RC ECO:0000313|Proteomes:UP000317041}; RA Lv Q., Li S.; RT "Draft genome sequencing of Psychrobacter sp. YGAH215."; RL Submitted (JUL-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 -!- 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:TSB23791.1}. 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; VKLR01000008; TSB23791.1; -; Genomic_DNA. DR AlphaFoldDB; A0A553Y3J7; -. DR UniPathway; UPA00068; UER00106. DR Proteomes; UP000317041; 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 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. DR TIGRFAMs; TIGR00120; ArgJ; 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..190 FT /note="Arginine biosynthesis bifunctional protein ArgJ FT alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5023536026" FT CHAIN 191..407 FT /note="Arginine biosynthesis bifunctional protein ArgJ beta FT chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5023536025" FT ACT_SITE 191 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 154 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 180 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 278 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 402 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 407 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT SITE 117 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 118 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 190..191 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" SQ SEQUENCE 407 AA; 43000 MW; 0D3C063D4E6B1ECF CRC64; MAVGNVAVPN TIYPIDGIKL SATAAGVRYK DRDDLVVIEI ADSANTAVVT TKNTFCAAPV RVLREHFAKA SPRYLITNTG NANAGTGADG KRRALDICAA LAAKAGVDVS SVLPFSTGVI GEPLNSDAII AGLDNALASL GADNWLVAAN GIRTTDTIPK LASEKVDVDA SSYHVTGMSK GSGMIRPNMA TMLGYVATDA NIAADLLQEM LSKINEQSFN RITVDGDTST NDCCVLIATG TASSEVIDSP EHPHYQPIFE ALTSVFVRLA QLIVRDGEGA TKFMTVKVTG GKTTQECCDV AYAVAHSPLV KTAFFASDAN WGRILAAVGY AGIDDLDTEQ VDVYLDEVMI CQNGGVAPSY TEAAGKEVMS RPEITINIDL ARGDAEDTVY TCDLSYDYVK INAEYRS //