ID A0A240TPU7_9BURK Unreviewed; 296 AA. AC A0A240TPU7; A0A240U095; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 08-MAY-2019, entry version 11. DE RecName: Full=Acetylglutamate kinase {ECO:0000256|HAMAP-Rule:MF_00082}; DE EC=2.7.2.8 {ECO:0000256|HAMAP-Rule:MF_00082}; DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00082}; DE AltName: Full=NAG kinase {ECO:0000256|HAMAP-Rule:MF_00082}; DE Short=NAGK {ECO:0000256|HAMAP-Rule:MF_00082}; GN Name=argB {ECO:0000256|HAMAP-Rule:MF_00082}; GN ORFNames=CBP33_02675 {ECO:0000313|EMBL:ART47163.1}, CBP34_02660 GN {ECO:0000313|EMBL:ART50790.1}; OS Acidovorax carolinensis. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=553814 {ECO:0000313|EMBL:ART47163.1, ECO:0000313|Proteomes:UP000194504}; RN [1] {ECO:0000313|EMBL:ART47163.1, ECO:0000313|Proteomes:UP000194432, ECO:0000313|Proteomes:UP000194504} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA2 {ECO:0000313|EMBL:ART47163.1}, and NA3 RC {ECO:0000313|EMBL:ART50790.1}; RA Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H., RA Wright F.A., Aitken M.D.; RT "Polyphasic characterization of four soil-derived phenanthrene- RT degrading Acidovorax strains and proposal of Acidovorax RT phenanthrenivorans sp. nov."; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl- CC L-glutamate. {ECO:0000256|HAMAP-Rule:MF_00082, CC ECO:0000256|SAAS:SAAS01159244}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5- CC phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; CC EC=2.7.2.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00082, CC ECO:0000256|SAAS:SAAS01124576}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 2/4. {ECO:0000256|HAMAP- CC Rule:MF_00082, ECO:0000256|SAAS:SAAS01090818}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082, CC ECO:0000256|SAAS:SAAS01159235}. CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00082, CC ECO:0000256|SAAS:SAAS01076971}. 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; CP021359; ART47163.1; -; Genomic_DNA. DR EMBL; CP021361; ART50790.1; -; Genomic_DNA. DR KEGG; acid:CBP33_02675; -. DR KEGG; acin:CBP34_02660; -. DR KO; K00930; -. DR BioCyc; GCF_002157145:CBP34_RS02660-MONOMER; -. DR UniPathway; UPA00068; UER00107. DR Proteomes; UP000194432; Chromosome. DR Proteomes; UP000194504; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule. DR CDD; cd04250; AAK_NAGK-C; 1. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_00082; ArgB; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR004662; AcgluKinase_fam. DR InterPro; IPR037528; ArgB. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR InterPro; IPR041727; NAGK-C. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF000728; NAGK; 1. DR PRINTS; PR00474; GLU5KINASE. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00761; argB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00082, KW ECO:0000256|SAAS:SAAS01090837}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00082, KW ECO:0000256|SAAS:SAAS01090853}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00082, KW ECO:0000256|SAAS:SAAS00088659}; KW Complete proteome {ECO:0000313|Proteomes:UP000194432, KW ECO:0000313|Proteomes:UP000194504}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082, KW ECO:0000256|SAAS:SAAS01159248}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00082, KW ECO:0000256|SAAS:SAAS00461199, ECO:0000313|EMBL:ART47163.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082, KW ECO:0000256|SAAS:SAAS00461200}; KW Reference proteome {ECO:0000313|Proteomes:UP000194432}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00082, KW ECO:0000256|SAAS:SAAS00461129}. FT DOMAIN 29 272 AA_kinase. {ECO:0000259|Pfam:PF00696}. FT REGION 69 70 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00082}. FT BINDING 91 91 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00082}. FT BINDING 193 193 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00082}. FT SITE 34 34 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00082}. FT SITE 253 253 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00082}. SQ SEQUENCE 296 AA; 31471 MW; 53A283D362EB71F0 CRC64; MTDLLSIAPR DKAEILAQAL PYIRKFHGKT MVIKYGGNAM TDPDLQADFA EDVVLLKLVG MNPVVVHGGG PQIETALNRL GKKGHFIQGM RVTDAETMEV VEWVLAGEVQ QDIVGLINQA GGKAVGLTGR DGGMIRAQKL KMVDNKDPSI EHDVGQVGDI VAIDPSVVKA LQDDAFIPVI SPIGFGENNE SYNINADVVA SKLATVLRAE KLMLLTNTPG VLDKAGKLLT DLTAREIDAL FADGTISGGM LPKIAGALDA ARAGVNAVHI IDGRVPHAML LEILTDQAYG TMIRSH //