ID D0U4I6_9GAMM Unreviewed; 394 AA. AC D0U4I6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 28-FEB-2018, entry version 43. DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {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 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 transacetylase {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 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=SUP05_FGYC13J70035 {ECO:0000313|EMBL:ACX30518.1}; OS uncultured SUP05 cluster bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Thioglobus; OC environmental samples. OX NCBI_TaxID=655186 {ECO:0000313|EMBL:ACX30518.1}; RN [1] {ECO:0000313|EMBL:ACX30518.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19900896; DOI=10.1126/science.1175309; RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., RA Tringe S.G., Tortell P.D., Hallam S.J.; RT "Metagenome of a versatile chemolithoautotroph from expanding oceanic RT dead zones."; RL Science 326:578-582(2009). 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: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L- CC glutamate. {ECO:0000256|HAMAP-Rule:MF_01106}. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L- CC ornithine + N-acetyl-L-glutamate. {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 --------------------------------------------------------------------------- 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; GQ351267; ACX30518.1; -; Genomic_DNA. DR MEROPS; T05.001; -. DR UniPathway; UPA00068; UER00106. 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; 3.60.70.12; -; 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 183 183 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 146 146 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 172 172 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 183 183 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 265 265 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 389 389 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 394 394 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT SITE 109 109 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 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 182 183 Cleavage; by autolysis. FT {ECO:0000256|HAMAP-Rule:MF_01106}. SQ SEQUENCE 394 AA; 42035 MW; 3311321E3D55C789 CRC64; MSQSLLNIEG VLSASIDAGI KNNDATDLSI IYLTESTVTA AVFTQNVFCA APVLVAKNHL NHHPKALLIN SGNANAGTGS QGMENTLHTC ACLAGELNIN TEQVLPFSTG VIGQQLELDK FNQGIPKVVV KLSTDAMGDV AKGILTTDLV EKTASKQFEV NGKTVTISGI AKGSGMIRPD MATMLSFIFT DVESTQAKLQ QCLTTSVNQS FNRITVDGDT STNDACTLSA TGASGVDIHD CVDEFQQALN EVTQSLAYQI IKDGEGATKF VEVCVKGGAS SEDCLEVAYT VAHSPLVKTA LFASDANWGR ILAAVGRANI SNLKIEDINI YLNEVSIIQA GEPDEHYTEE AGSNEMAKEE IIITIEIGKG DAQESVWTTD FSYDYVKINA EYRT //