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
Functions
acetylglutamate kinase activity / ATP binding
Processes
arginine biosynthetic process / cellular response to DNA damage stimulus
Components
cytoplasm
General Function
Atp binding
Specific Function
Not Available
Pfam Domain Function
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
ResourceLink
UniProtKB IDP0A6C8
UniProtKB Entry NameARGB_ECOLI
GenBank Protein ID145334
GenBank Gene IDM21446
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04075N-Acetyl-L-GlutamateexperimentalunknownDetails
DB04395Phosphoaminophosphonic Acid-Adenylate EsterexperimentalunknownDetails
DB04444Tetrafluoroaluminate IonexperimentalunknownDetails