ID A0A354GZR2_9BACT Unreviewed; 399 AA. AC A0A354GZR2; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 05-DEC-2018, 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 ORFNames=DDY78_27150 {ECO:0000313|EMBL:HBI46500.1}; OS Planctomycetales bacterium. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC unclassified Planctomycetales (miscellaneous). OX NCBI_TaxID=2053591 {ECO:0000313|EMBL:HBI46500.1}; RN [1] {ECO:0000313|EMBL:HBI46500.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA11822 {ECO:0000313|EMBL:HBI46500.1}; RX PubMed=30148503; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 0:0-0(2018). 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:HBI46500.1}. 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; DNTJ01000545; HBI46500.1; -; Genomic_DNA. DR UniPathway; UPA00068; UER00106. 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_sf. 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01106}. FT ACT_SITE 186 186 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 149 149 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 175 175 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 186 186 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 271 271 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 394 394 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 399 399 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT SITE 110 110 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 111 111 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 185 186 Cleavage; by autolysis. FT {ECO:0000256|HAMAP-Rule:MF_01106}. SQ SEQUENCE 399 AA; 42309 MW; E63D81F268AA7F33 CRC64; MNNWHLARGY RFAGVHSGIR PDPDRLDLAL IVSDAPAAAA GAFTQNRVRA APVRVCQERL PAEDVRGVVV CSGNANACTG QRGLDDARRM TVVAAETVGC RPTQMLVCST GVIGQFLPMQ AIEPGIRAAA DVLTATPDAL DAAARAILTT DTRIKVVTKT ISIDNIEVRL TGVAKGAAMI GPNLATMLAF VFTDAAVSAV DLAPLTVRAA DQSFNCVSVE GHTSTNDTLL LFANGQASAG RPLSGEALGQ FSDAATGVCR ELAQAIAADA EGATHLIVID VEGLRDDDEA RRVAKTIAES ALVKTAVFGA DPNWGRIVSA AGYAGVEFEE EQLSLWMGDL LLYHAGAPQP FEAEAASAYL KRERTIHLRL RFTLGAGRCT FWTCDLTHEY IRLNAEYTT //