ID A0A1L7HZX0_9FLAO Unreviewed; 258 AA. AC A0A1L7HZX0; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 13-SEP-2023, entry version 27. 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=GRFL_0165 {ECO:0000313|EMBL:APU66889.1}; OS Christiangramia flava JLT2011. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Christiangramia. OX NCBI_TaxID=1229726 {ECO:0000313|EMBL:APU66889.1, ECO:0000313|Proteomes:UP000186230}; RN [1] {ECO:0000313|EMBL:APU66889.1, ECO:0000313|Proteomes:UP000186230} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JLT2011 {ECO:0000313|EMBL:APU66889.1, RC ECO:0000313|Proteomes:UP000186230}; RA Tang K.; RT "Multi-omics approach to identify versatile polysaccharide utilization RT systems of a marine flavobacterium Gramella flava."; RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- CC glutamate. {ECO:0000256|HAMAP-Rule:MF_00082}. 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; EC=2.7.2.8; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00082}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- CC L-ornithine from L-glutamate: step 2/4. {ECO:0000256|HAMAP- CC Rule:MF_00082}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082}. CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00082}. 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; CP016359; APU66889.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1L7HZX0; -. DR STRING; 1229726.GRFL_0165; -. DR EnsemblBacteria; APU66889; APU66889; GRFL_0165. DR KEGG; gfl:GRFL_0165; -. DR OrthoDB; 9803155at2; -. DR UniPathway; UPA00068; UER00107. DR Proteomes; UP000186230; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd04238; AAK_NAGK-like; 1. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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 NCBIfam; TIGR00761; argB; 1. DR PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1. DR PANTHER; PTHR23342:SF0; N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF000728; NAGK; 1. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00082}; KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP- KW Rule:MF_00082}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00082}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000313|EMBL:APU66889.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082}; KW Reference proteome {ECO:0000313|Proteomes:UP000186230}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000313|EMBL:APU66889.1}. FT DOMAIN 4..240 FT /note="Aspartate/glutamate/uridylate kinase" FT /evidence="ECO:0000259|Pfam:PF00696" FT BINDING 40..41 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082" FT BINDING 62 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082" FT BINDING 157 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082" FT SITE 8 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082" FT SITE 223 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082" SQ SEQUENCE 258 AA; 28296 MW; E9503A67C706FEF5 CRC64; MKQLKVIKIG GKLIEDEGKL ADFLNDFAKL KGPKILVHGG GNMATEIAGK LGYETKMVDG RRITDENSMA VITMVYGGLI NKNIVAKLQN RNVNAIGLCG ADGKAIVSKK RPVKEIDFGF VGDIENINSE FILNLLEQGI TPVFSAISYS ETGELFNTNA DSVASEIAVA MSKEMETELL YCFEKKGVLA DIDNETSIIE KIDAEEYQSL LEQKVISDGM LPKLHNCFQA IEKGVQTVRL GDMHLLRPES KHTKILSS //