ID A0A553Y3J7_9GAMM Unreviewed; 407 AA. AC A0A553Y3J7; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, entry version 2. 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; Pseudomonadales; OC Moraxellaceae; 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 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 -!- 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: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 UniPathway; UPA00068; UER00106. DR Proteomes; UP000317041; Unassembled WGS sequence. 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:TSB23791.1}; 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:UP000317041}; 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:TSB23791.1}. FT ACT_SITE 191 191 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 154 154 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 180 180 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 191 191 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 278 278 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 402 402 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 407 407 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT SITE 117 117 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 118 118 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 190 191 Cleavage; by autolysis. FT {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 //