ID C5QSR6_9STAP Unreviewed; 397 AA. AC C5QSR6; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 31-JAN-2018, entry version 46. 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 beta chain {ECO:0000256|HAMAP-Rule:MF_01106}; DE Contains: DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000256|HAMAP-Rule:MF_01106}; GN Name=argJ {ECO:0000256|HAMAP-Rule:MF_01106, GN ECO:0000313|EMBL:EES39986.1}; GN ORFNames=HMPREF0793_2272 {ECO:0000313|EMBL:EES39986.1}; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=525378 {ECO:0000313|EMBL:EES39986.1, ECO:0000313|Proteomes:UP000003152}; RN [1] {ECO:0000313|EMBL:EES39986.1, ECO:0000313|Proteomes:UP000003152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23864:W1 {ECO:0000313|EMBL:EES39986.1, RC ECO:0000313|Proteomes:UP000003152}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. 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 -!- 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:EES39986.1}. 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; ACJB01000064; EES39986.1; -; Genomic_DNA. DR RefSeq; WP_002443058.1; NZ_GG696773.1. DR STRING; 525378.HMPREF0793_2272; -. DR EnsemblBacteria; EES39986; EES39986; HMPREF0793_2272. DR eggNOG; ENOG4105C5V; Bacteria. DR eggNOG; COG1364; LUCA. DR OrthoDB; POG091H070E; -. DR UniPathway; UPA00068; UER00106. DR Proteomes; UP000003152; Unassembled WGS sequence. 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 TIGRFAMs; TIGR00120; ArgJ; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01106, KW ECO:0000313|EMBL:EES39986.1}; 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 Complete proteome {ECO:0000313|Proteomes:UP000003152}; 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, KW ECO:0000313|EMBL:EES39986.1}. FT ACT_SITE 184 184 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 147 147 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 173 173 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 184 184 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 270 270 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 392 392 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT BINDING 397 397 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01106}. FT SITE 113 113 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 114 114 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 183 184 Cleavage; by autolysis. FT {ECO:0000256|HAMAP-Rule:MF_01106}. SQ SEQUENCE 397 AA; 42750 MW; BDA5D98A525DAC00 CRC64; MKVIEGNIAS PLGFSADGLH AGFKRKKLDF GWIVSEVPAN VAGVFTTNKV IAAPLILTQS CIENEGQMQA IVVNSGIANS CTGEQGLRDA QTMQQWAAEK LHIKKEYVGV ASTGVIGEMM PMNILENGFS KLVINGNADD FAKSILTTDK DTKTCVVTET FDKDIVTTAG VAKGSGMIHP NMATMLAFIT CDANISTQTL QQALSEIVQI TFNQITVDGD TSTNDMVIVM SNGCTNNKEI LPNTSDYTKF KAMLFHVMQD LAKKIAKDGE GATKLIEVNV TGAQNSESAR MIAKCIVGSS LVKTAIFGED PNWGRIIAAA GYADTTFNPN QIDIAIGNIT VLSKSTPIHF DKEEMQDIMS KDEVTIHMNL NGGQCEGKAW GCDLSYDYVK INALYTT //