Acetylglutamate kinase (P0A6C8)

Identification
Name:Acetylglutamate kinase
Synonyms:
  • N-acetyl-L-glutamate 5-phosphotransferase
  • NAG kinase
  • AGK
Gene Name:argB
Enzyme Class:
Biological Properties
General Function:Involved in acetylglutamate kinase activity
Specific Function:ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L- glutamate 5-phosphate
Cellular Location:Cytoplasm (Probable)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetyl-L-alanine + 1.0Adenosine triphosphate + 1.0N-Acetylglutamic acid ↔ 1.0N-Acetyl-L-glutamyl 5-phosphate + 1.0ADP
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0N-Acetyl-L-alanine ↔ 1.0ADP + 1.0N-Acetyl-L-glutamyl 5-phosphate
ReactionCard
SMPDB Reactions:
1.0N-Acetylglutamic acid+1.0Thumb+1.0Thumb → 1.0Adenosine diphosphate+1.0Thumb+1.0Thumb
1.0N-Acetylglutamic acid + 1.0Adenosine triphosphate + 1.0N-Acetylglutamic acid → 1.0Adenosine diphosphate + 1.0N-Acetyl-L-glutamyl 5-phosphate + 1.0ADP
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01138N-Acetyl-L-alanineMetaboCard
ECMDB06456N-Acetyl-L-glutamyl 5-phosphateMetaboCard
ECMDB21429N-Acetylglutamic acidMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
acetylglutamate kinase activity
catalytic activity
kinase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
arginine biosynthetic process
arginine metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
metabolic process
Gene Properties
Blattner:b3959
Gene OrientationClockwise
Centisome Percentage:89.53
Left Sequence End4154036
Right Sequence End4154812
Gene Sequence:
>777 bp
ATGTTACGTTTCTCTGCTAATTTATCGATGTTATTTGGAGAATATGATTTTCTCGCCCGT
TTTGAGAAAGCTGCGCAGTGTGGTTTTCGCGGCGTTGAATTTATGTTTCCTTATGACTAC
GACATTGAAGAATTAAAACATGTGCTGGCGAGTAATAAACTCGAACATACGCTGCACAAT
TTACCGGCGGGTGACTGGGCGGCGGGGGAGCGCGGTATTGCCTGTATTCCTGGCCGTGAA
GAAGAGTTTCGGGATGGCGTAGCAGCAGCGATTCGTTATGCCCGTGCGCTGGGTAATAAA
AAAATTAACTGTCTGGTCGGTAAAACGCCGGCTGGTTTCAGCAGTGAACAGATTCACGCA
ACGCTTGTAGAAAACCTGCGTTATGCCGCGAATATGCTGATGAAAGAAGATATTTTATTA
CTGATTGAACCTATTAACCATTTTGATATTCCTGGTTTCCATCTCACCGGAACTCGGCAG
GCGCTGAAATTGATTGATGATGTTGGTTGCTGCAATTTGAAAATTCAGTATGACATTTAT
CATATGCAGCGGATGGAAGGTGAATTAACCAACACCATGACTCAGTGGGCTGATAAAATT
GGTCACCTGCAAATTGCCGATAATCCGCATCGCGGCGAACCGGGAACCGGAGAAATTAAT
TATGATTATCTCTTTAAGGTAATCGAAAATTCTGACTACAACGGTTGGGTTGGGTGTGAA
TATAAACCCCAAACCACCACGGAAGCCGGTTTACGCTGGATGGATCCGTACCGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:258
Protein Molecular Weight:27159
Protein Theoretical pI:5
PDB File:1OHB
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Acetylglutamate kinase
MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVIVHGGGCVVDELMKGLNLPVK
KKNGLRVTPADQIDIITGALAGTANKTLLAWAKKHQIAAVGLFLGDGDSVKVTQLDEELG
HVGLAQPGSPKLINSLLENGYLPVVSSIGVTDEGQLMNVNADQAATALAATLGADLILLS
DVSGILDGKGQRIAEMTAAKAEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHA
EQLPALFNGMPMGTRILA
References
External Links:
ResourceLink
Uniprot ID:P0A6C8
Uniprot Name:ARGB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674646
PDB ID:1OHB
Ecogene ID:EG10064
Ecocyc:EG10064
ColiBase:b3959
Kegg Gene:b3959
EchoBASE ID:EB0062
CCDB:ARGB_ECOLI
BacMap:145698337
General Reference:
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • 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 55:1350-1352. Pubmed: 10393305
  • 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 331:231-244. Pubmed: 12875848
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • 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 334:459-476. Pubmed: 14623187
  • Parsot, C., Boyen, A., Cohen, G. N., Glansdorff, N. (1988). "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 68:275-283. Pubmed: 2851495
  • 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 10:329-342. Pubmed: 12005432