ID D0U4I6_9GAMM Unreviewed; 394 AA. AC D0U4I6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 31-OCT-2012, entry version 12. DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ 1; GN Name=argJ1; ORFNames=SUP05_FGYC13J70035; OS uncultured SUP05 cluster bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC unclassified Oceanospirillales; SUP05 cluster; environmental samples. OX NCBI_TaxID=655186; RN [1] RP NUCLEOTIDE SEQUENCE. 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 oxygen RT minimum 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 CC acetylglutamate from glutamate and acetyl-CoA, and of ornithine by CC transacetylation between acetylornithine and glutamate (By CC similarity). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L- CC glutamate. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L- CC ornithine + N-acetyl-L-glutamate. 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. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 1/4. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e., CC capable of catalyzing only the fifth step of the arginine CC biosynthetic pathway (By similarity). CC -!- SIMILARITY: Belongs to the ArgJ family. 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 UniPathway; UPA00068; UER00106. DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:InterPro. DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:InterPro. DR HAMAP; MF_01106; ArgJ; 1; -. DR InterPro; IPR002813; Arg_biosynth_ArgJ. DR InterPro; IPR016117; Pept_S58_DmpA/Arg_biosyn_ArgJ. DR PANTHER; PTHR23100; PTHR23100; 1. DR Pfam; PF01960; ArgJ; 1. DR ProDom; PD004193; Arg_biosynth_ArgJ; 1. DR SUPFAM; SSF56266; Pept_S58_DmpA/Arg_biosyn_ArgJ; 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 Transferase. FT SITE 182 183 Cleavage; by autolysis (By similarity). 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 //