MetaCyc Enzyme: acetylglutamate kinase

Gene: argB Accession Numbers: EG10064 (MetaCyc), b3959, ECK3950

Synonyms: N-acetylglutamate kinase, N-acetylglutamokinase, NAG kinase, AGK, ATP:N-acetyl-L-glutamate 5-phosphotransferase

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of acetylglutamate kinase = [ArgB]2
         acetylglutamate kinase monomer = ArgB

Acetylglutamate kinase (ArgB) catalyzes the second step in ornithine and arginine biosynthesis.

ArgB catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate to generate N-acetylglutamyl-phosphate, with a specific activity of 1.1 µmol/s/mg [Gil99].

Acetylglutamate kinase comprises a homodimer of ArgB monomers, each of which lacks its amino-terminal methionine [Gil99].

Acetylglutamate kinase has been crystallized on its own, as well as bound to N-acetyl-L-glutamate, an ATP analong, ADP and a transition state analog [RamonMaiques02, GilOrtiz02]. The catalytic mechanism proposed based on these structures has been evaluated via site-directed mutagenesis [GilOrtiz03].

Locations: cytosol

Map Position: [4,154,039 -> 4,154,812]

Molecular Weight of Polypeptide: 27.028 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0012967 , CGSC:1020 , DIP:DIP-9136N , EchoBASE:EB0062 , EcoGene:EG10064 , EcoliWiki:b3959 , Entrez-gene:948464 , Mint:MINT-1309378 , ModBase:P0A6C8 , OU-Microarray:b3959 , PortEco:argB , PR:PRO_000022127 , Pride:P0A6C8 , Protein Model Portal:P0A6C8 , RefSeq:NP_418394 , RegulonDB:EG10064 , SMR:P0A6C8 , String:511145.b3959 , UniProt:P0A6C8

Relationship Links: InterPro:IN-FAMILY:IPR001048 , InterPro:IN-FAMILY:IPR004662 , PDB:Structure:1GS5 , PDB:Structure:1GSJ , PDB:Structure:1OH9 , PDB:Structure:1OHA , PDB:Structure:1OHB , PDB:Structure:2WXB , PDB:Structure:2X2W , Pfam:IN-FAMILY:PF00696

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006526 - arginine biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA06, GOA01, Takahara07]
GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0008652 - cellular amino acid biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0003991 - acetylglutamate kinase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Gil99]
GO:0042803 - protein homodimerization activity Inferred from experiment [Gil99]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids arginine

Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Enzymatic reaction of: acetylglutamate kinase

EC Number:

N-acetyl-L-glutamate + ATP <=> N-acetylglutamyl-phosphate + ADP

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: superpathway of arginine and polyamine biosynthesis , L-arginine biosynthesis I (via L-ornithine) , L-ornithine biosynthesis

Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Cofactors or Prosthetic Groups: Mg2+ [Gil99]

Kinetic Parameters:

Km (μM)
[GilOrtiz10, BRENDA14]
[MarcoMarin03, BRENDA14]
[GilOrtiz10, BRENDA14]
290.0, 300.0
[MarcoMarin03, BRENDA14]

Sequence Features

Feature Class Location Citations Comment
Amino-Acid-Site 8
UniProt: Transition state stabilizer; Sequence Annotation Type: site.
Mutagenesis-Variant 8
[MarcoMarin03, UniProt11]
UniProt: Reduces activity 50-fold. Increases KM for N-acetyl-L-glutamate and ATP about 10-fold.
Amino-Acid-Sites-That-Bind 66
[GilOrtiz03, RamonMaiques02, UniProt15]
UniProt: Substrate.
Mutagenesis-Variant 66
[MarcoMarin03, UniProt11]
UniProt: Increases KM for N-acetyl-L- glutamate over 1000-fold. Increases KM for ATP nearly 20-fold.
Amino-Acid-Sites-That-Bind 158
[GilOrtiz03, RamonMaiques02, UniProt15]
UniProt: Substrate.
Mutagenesis-Variant 158
[MarcoMarin03, UniProt11]
UniProt: Increases KM for N-acetyl-L- glutamate over 1000-fold. Increases KM for ATP over 20-fold.
Mutagenesis-Variant 162
[MarcoMarin03, UniProt11]
UniProt: Reduces activity over 99%. No effect on KM for N-acetyl-L-glutamate and ATP.
Amino-Acid-Site 217
UniProt: Transition state stabilizer; Sequence Annotation Type: site.

Peter D. Karp on Wed Jan 18, 2006:
Gene left-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
10/20/97 Gene b3959 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10064.


BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014."

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gil99: Gil F, Ramon-Maiques S, Marina A, Fita I, Rubio V (1999). "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;55 ( Pt 7);1350-2. PMID: 10393305

GilOrtiz02: Gil-Ortiz F, Fita I, Ramon-Maiques S, Marina A, Rubio V (2002). "A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a protein surface: external and internal AMPPNP molecules in crystalline N-acetyl-L-glutamate kinase." Acta Crystallogr D Biol Crystallogr 58(Pt 10 Pt 2);1892-5. PMID: 12351849

GilOrtiz03: Gil-Ortiz F, Ramon-Maiques S, Fita I, Rubio V (2003). "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 331(1);231-44. PMID: 12875848

GilOrtiz10: Gil-Ortiz F, Ramon-Maiques S, Fernandez-Murga ML, Fita I, Rubio V (2010). "Two crystal structures of Escherichia coli N-acetyl-L-glutamate kinase demonstrate the cycling between open and closed conformations." J Mol Biol 399(3);476-90. PMID: 20403363

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

MarcoMarin03: Marco-Marin C, Ramon-Maiques S, Tavarez S, Rubio V (2003). "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 334(3);459-76. PMID: 14623187

RamonMaiques02: Ramon-Maiques S, Marina A, Gil-Ortiz F, Fita I, Rubio V (2002). "Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis." Structure (Camb) 10(3);329-42. PMID: 12005432

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

Takahara07: Takahara K, Akashi K, Yokota A (2007). "Continuous spectrophotometric assays for three regulatory enzymes of the arginine biosynthetic pathway." Anal Biochem 368(2);138-47. PMID: 17651682

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Sun Oct 4, 2015, biocyc13.