ID A0A7C6K5Y9_9FIRM Unreviewed; 405 AA. AC A0A7C6K5Y9; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 07-APR-2021, entry version 3. 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:HHV34006.1}; GN ORFNames=GXX59_00260 {ECO:0000313|EMBL:HHV34006.1}; OS Syntrophomonadaceae bacterium. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae. OX NCBI_TaxID=2093811 {ECO:0000313|EMBL:HHV34006.1}; RN [1] {ECO:0000313|EMBL:HHV34006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AS05jafATM_105 {ECO:0000313|EMBL:HHV34006.1}; RX PubMed=32123542; RA Campanaro S., Treu L., Rodriguez-R L.M., Kovalovszki A., Ziels R.M., RA Maus I., Zhu X., Kougias P.G., Basile A., Luo G., Schluter A., RA Konstantinidis K.T., Angelidaki I.; RT "New insights from the biogas microbiome by comprehensive genome-resolved RT metagenomics of nearly 1600 species originating from multiple anaerobic RT digesters."; RL Biotechnol. Biofuels 13:25-20(2020). 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:HHV34006.1}. 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; DUMY01000010; HHV34006.1; -; Genomic_DNA. 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; 3.10.20.340; -; 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|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..191 FT /note="Arginine biosynthesis bifunctional protein ArgJ FT alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5028541708" FT CHAIN 192..405 FT /note="Arginine biosynthesis bifunctional protein ArgJ beta FT chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT /id="PRO_5028541707" FT ACT_SITE 192 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 155 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 181 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 192 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 278 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 400 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" FT BINDING 405 FT /note="Substrate" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01106" FT SITE 191..192 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106" SQ SEQUENCE 405 AA; 42696 MW; 0DD1B663E4CB7721 CRC64; MSQQLKYKEI SGGVTTPQGF LAAGVTAGVR KNRQRDVALL YSEIPATAAA VYTQNQVKAA PVLVTQEHLS GGSAQAVVVN SGIANACTGE QGLTDARMMA KLAGDALEIP VEHVAVASTG VIGEYLPMER IQSGIKEAAR LLSTEGGAAA EAILTTDTVT KEYAIQFNLG GREVKVGGMA KGSGMIHPNM ATMLAFITTD ACVEQQALKL ALCWAVDRSF NNITVDGDTS TNDMVVTLAN GQAGNPLISA DQPEFNLFRE AVYIVCVELA KMIARDGEGA SKLLEVQVKN AASEKEARII ARSIASSSLV KTAVFGEDTN WGRVLSAAGA CGVVFDPNMV DVYLGDILVA AEGRGLPFDE KRADAILQES DVTITVDLHK GTATGIAWGC DLTFDYIKIN ADYRT //