ID A0A240TPU7_9BURK Unreviewed; 296 AA. AC A0A240TPU7; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 22-NOV-2017, entry version 2. DE RecName: Full=Acetylglutamate kinase {ECO:0000256|SAAS:SAAS00919237}; DE EC=2.7.2.- {ECO:0000256|SAAS:SAAS00919236}; DE EC=2.7.2.8 {ECO:0000256|SAAS:SAAS00919231}; GN ORFNames=CBP33_02675 {ECO:0000313|EMBL:ART47163.1}; OS Acidovorax sp. NA2. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=1662456 {ECO:0000313|EMBL:ART47163.1, ECO:0000313|Proteomes:UP000194504}; RN [1] {ECO:0000313|EMBL:ART47163.1, ECO:0000313|Proteomes:UP000194504} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA2 {ECO:0000313|EMBL:ART47163.1}; 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|SAAS:SAAS00701626}. CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L- CC glutamate 5-phosphate. {ECO:0000256|SAAS:SAAS00384289}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 2/4. CC {ECO:0000256|SAAS:SAAS00384237}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00919239}. CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB CC subfamily. {ECO:0000256|SAAS:SAAS00701617}. 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 UniPathway; UPA00068; UER00107. DR Proteomes; UP000194504; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_00082_B; ArgB_B; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR004662; AcgluKinase. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR001057; Glu/AcGlu_kinase. 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|SAAS:SAAS00701594}; KW Arginine biosynthesis {ECO:0000256|SAAS:SAAS00088592}; KW ATP-binding {ECO:0000256|SAAS:SAAS00651454}; KW Complete proteome {ECO:0000313|Proteomes:UP000194504}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00919233}; KW Kinase {ECO:0000256|SAAS:SAAS00651459, ECO:0000313|EMBL:ART47163.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00651462}; KW Transferase {ECO:0000256|SAAS:SAAS00651468}. FT DOMAIN 29 272 AA_kinase. {ECO:0000259|Pfam:PF00696}. 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 //