ID ARGJ_NEIG1 Reviewed; 406 AA. AC Q5F7I3; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 02-DEC-2020, entry version 97. DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000255|HAMAP-Rule:MF_01106}; DE Includes: DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106}; DE EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_01106}; DE AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Short=OATase {ECO:0000255|HAMAP-Rule:MF_01106}; DE AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Includes: DE RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106}; DE EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01106}; DE AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Short=AGSase {ECO:0000255|HAMAP-Rule:MF_01106}; DE Contains: DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_01106}; DE Contains: DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_01106}; GN Name=argJ {ECO:0000255|HAMAP-Rule:MF_01106}; OrderedLocusNames=NGO1194; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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:0000255|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:0000255|HAMAP-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:0000255|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:0000255|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:0000255|HAMAP- CC Rule:MF_01106}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. CC {ECO:0000255|HAMAP-Rule:MF_01106}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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. CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|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; AE004969; AAW89854.1; -; Genomic_DNA. DR RefSeq; WP_003691802.1; NC_002946.2. DR RefSeq; YP_208266.1; NC_002946.2. DR SMR; Q5F7I3; -. DR EnsemblBacteria; AAW89854; AAW89854; NGO_1194. DR GeneID; 50372573; -. DR KEGG; ngo:NGO1194; -. DR PATRIC; fig|242231.10.peg.1401; -. DR HOGENOM; CLU_027172_1_0_4; -. DR OMA; GMIAPNM; -. DR BioCyc; NGON242231:G1FZ9-1067-MONOMER; -. DR UniPathway; UPA00068; UER00106. DR UniPathway; UPA00068; UER00111. DR Proteomes; UP000000535; Chromosome. 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; -; 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; Amino-acid biosynthesis; Arginine biosynthesis; KW Autocatalytic cleavage; Cytoplasm; Multifunctional enzyme; KW Reference proteome; Transferase. FT CHAIN 1..189 FT /note="Arginine biosynthesis bifunctional protein ArgJ FT alpha chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT /id="PRO_0000227234" FT CHAIN 190..406 FT /note="Arginine biosynthesis bifunctional protein ArgJ beta FT chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT /id="PRO_0000227235" FT ACT_SITE 190 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT BINDING 152 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT BINDING 179 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT BINDING 190 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT BINDING 277 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT BINDING 401 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT BINDING 406 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT SITE 119 FT /note="Involved in the stabilization of negative charge on FT the oxyanion by the formation of the oxyanion hole" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT SITE 120 FT /note="Involved in the stabilization of negative charge on FT the oxyanion by the formation of the oxyanion hole" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" FT SITE 189..190 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106" SQ SEQUENCE 406 AA; 42851 MW; A3F3635905E2C856 CRC64; MAVNLTEKTA EQLPDIDGIA LYTAQAGVKK PGHTDLTLIA VAAGSTVGAV FTTNRFCAAP VHIAKSHLFD EDGVRALVIN TGNANAGTGA QGRIDALAVC AAAARQIGCK PNQVMPFSTG VILEPLPADK IIAALPKMQP AFWNEAARAI MTTDTVPKAA SREGKVGDQH TVRATGIAKG SGMIHPNMAT MLGFIATDAK VSQPVLQLMT QEIADETFNT ITVDGDTSTN DSFVIIATGK NSQSEIDNIA DPRYAQLKEL LCSLALELAQ AIVRDGEGAT KFITVRVENA KTCDEARQAA YAAARSPLVK TAFFASDPNL GRLLAAIGYA DVADLDTDLV EMYLDDILVA EHGGRAASYT EAQGQAVMSK DEITVRIKLH RGQAAATVYT CDLSHGYVSI NADYRS //