Acetylglutamate kinase
Details
- Name
- Acetylglutamate kinase
- Synonyms
- 2.7.2.8
- AGK
- N-acetyl-L-glutamate 5-phosphotransferase
- NAG kinase
- Gene Name
- argB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0003154|Acetylglutamate kinase MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVIVHGGGCVVDELMKGLNLPVK KKNGLRVTPADQIDIITGALAGTANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELG HVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNADQAATALAATLGADLILLS DVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHA EQLPALFNGMPMGTRILA
- Number of residues
- 258
- Molecular Weight
- 27159.285
- Theoretical pI
- 5.32
- GO Classification
- Functionsacetylglutamate kinase activity / ATP bindingProcessesarginine biosynthetic process / cellular response to DNA damage stimulusComponentscytoplasm
- General Function
- Atp binding
- Specific Function
- Not Available
- Pfam Domain Function
- AA_kinase (PF00696)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011126|Acetylglutamate kinase (argB) ATGAATCCATTAATTATCAAACTGGGCGGCGTACTGCTGGATAGTGAAGAGGCGCTGGAA CGTCTGTTTAGCGCACTGGTGAATTATCGTGAGTCACATCAGCGTCCGCTGGTGATTGTG CACGGCGGCGGTTGCGTGGTGGATGAGCTGATGAAAGGGCTGAATCTGCCGGTGAAAAAG AAAAACGGCCTGCGGGTGACGCCTGCTGATCAGATAGACATTATCACCGGAGCACTGGCG GGAACGGCAAATAAAACCCTGTTGGCATGGGCGAAGAAACATCAGATTGCGGCCGTAGGT TTGTTTCTCGGTGACGGCGACAGCGTCAAAGTGACCCAGCTTGATGAAGAGTTAGGTCAT GTTGGACTGGCGCAGCCAGGTTCGCCTAAGCTTATCAACTCCTTGCTGGAGAACGGTTAT CTGCCGGTGGTCAGCTCCATTGGCGTAACAGACGAAGGGCAACTGATGAACGTCAATGCC GACCAGGCGGCAACGGCGCTGGCGGCAACGCTGGGCGCGGATCTGATTTTGCTCTCCGAC GTCAGCGGCATTCTCGACGGCAAAGGGCAACGCATTGCCGAAATGACCGCCGCGAAAGCA GAACAACTGATTGAGCAGGGCATTATTACTGACGGCATGATAGTGAAAGTGAACGCGGCG CTGGATGCGGCCCGCACGCTGGGCCGTCCGGTAGATATCGCCTCCTGGCGTCATGCGGAG CAGCTTCCGGCACTGTTTAACGGTATGCCGATGGGTACGCGGATTTTAGCTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A6C8 UniProtKB Entry Name ARGB_ECOLI GenBank Protein ID 145334 GenBank Gene ID M21446 - General References
- Parsot C, Boyen A, Cohen GN, Glansdorff N: Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologous and analogous enzymes. Gene. 1988 Sep 7;68(2):275-83. [Article]
- Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Marco-Marin C, Ramon-Maiques S, Tavarez S, Rubio V: Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase. J Mol Biol. 2003 Nov 28;334(3):459-76. [Article]
- Gil F, Ramon-Maiques S, Marina A, Fita I, Rubio V: N-Acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms. Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1350-2. [Article]
- Ramon-Maiques S, Marina A, Gil-Ortiz F, Fita I, Rubio V: Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis. Structure. 2002 Mar;10(3):329-42. [Article]
- Gil-Ortiz F, Ramon-Maiques S, Fita I, Rubio V: The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic. J Mol Biol. 2003 Aug 1;331(1):231-44. [Article]