Acetylornithine deacetylase (P23908)

Identification
Name:Acetylornithine deacetylase
Synonyms:
  • AO
  • Acetylornithinase
  • N-acetylornithinase
  • NAO
Gene Name:argE
Enzyme Class:
Biological Properties
General Function:Involved in zinc ion binding
Specific Function:Displays a broad specificity and can also deacylate substrates such as acetylarginine, acetylhistidine or acetylglutamate semialdehyde
Cellular Location:Cytoplasm (Probable)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0N-Acetylornithine + 1.0Water ↔ 1.0Acetic acid + 1.0Ornithine + 1.0L-Ornithine
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetylornithine + 1.0Water ↔ 1.0Acetic acid + 1.0Ornithine
ReactionCard
1.0N-Acetyl-L-citrulline+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetyl-L-citrulline + 1.0Water ↔ 1.0Acetic acid + 1.0Citrulline
ReactionCard
SMPDB Reactions:
1.0N-acetyl-L-glutamate+1.0L-Glutamic acid+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-acetyl-L-glutamate + 1.0L-Glutamic acid + 1.0L-Glutamate → 1.0Oxoglutaric acid + 1.0N-Acetylornithine
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0L-Ornithine monochlorohydrate/ornithine
1.0N-Acetylornithine + 1.0Water → 1.0Acetic acid + 1.0L-Ornithine monochlorohydrate/ornithine
ReactionCard
1.0Thumb+1.0Thumb → 1.0Ornithine+1.0Thumb+1.0Thumb
1.0N-Acetylornithine + 1.0Water → 1.0Ornithine + 1.0Acetic acid + 1.0Ornithine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0N-Acetylornithine + 1.0Water ↔ 1.0Acetic acid + 1.0Ornithine + 1.0L-Ornithine
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-Acetyl-L-glutamate 5-semialdehyde + 1.0Water → 1.0Acetic acid + 1.0L-Glutamic-gamma-semialdehyde
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00042Acetic acidMetaboCard
ECMDB00904CitrullineMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB01305L-Glutamic-gamma-semialdehydeMetaboCard
ECMDB23898L-OrnithineMetaboCard
ECMDB06488N-Acetyl-L-glutamate 5-semialdehydeMetaboCard
ECMDB03357N-AcetylornithineMetaboCard
ECMDB00214OrnithineMetaboCard
ECMDB04123Oxoglutaric acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
acetylornithine deacetylase activity
binding
catalytic activity
cation binding
cobalt ion binding
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
ion binding
metal ion binding
metallopeptidase activity
peptidase activity
peptidase activity, acting on L-amino acid peptides
protein binding
transition metal ion binding
zinc ion binding
Process
arginine biosynthetic process
arginine metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
macromolecule metabolic process
metabolic process
protein metabolic process
proteolysis
Gene Properties
Blattner:b3957
Gene OrientationCounterclockwise
Centisome Percentage:89.48
Left Sequence End4151719
Right Sequence End4152870
Gene Sequence:
>1152 bp
ATGTTTGAACCAATGGAACTTACCAATGACGCGGTGATTAAAGTCATCGGCGTCGGCGGC
GGCGGCGGTAATGCTGTTGAACACATGGTGCGCGAGCGCATTGAAGGTGTTGAATTCTTC
GCGGTAAATACCGATGCACAAGCGCTGCGTAAAACAGCGGTTGGACAGACGATTCAAATC
GGTAGCGGTATCACCAAAGGACTGGGCGCTGGCGCTAATCCAGAAGTTGGCCGCAATGCG
GCTGATGAGGATCGCGATGCATTGCGTGCGGCGCTGGAAGGTGCAGACATGGTCTTTATT
GCTGCGGGTATGGGTGGTGGTACCGGTACAGGTGCAGCACCAGTCGTCGCTGAAGTGGCA
AAAGATTTGGGTATCCTGACCGTTGCTGTCGTCACTAAGCCTTTCAACTTTGAAGGCAAG
AAGCGTATGGCATTCGCGGAGCAGGGGATCACTGAACTGTCCAAGCATGTGGACTCTCTG
ATCACTATCCCGAACGACAAACTGCTGAAAGTTCTGGGCCGCGGTATCTCCCTGCTGGAT
GCGTTTGGCGCAGCGAACGATGTACTGAAAGGCGCTGTGCAAGGTATCGCTGAACTGATT
ACTCGTCCGGGTTTGATGAACGTGGACTTTGCAGACGTACGCACCGTAATGTCTGAGATG
GGCTACGCAATGATGGGTTCTGGCGTGGCGAGCGGTGAAGACCGTGCGGAAGAAGCTGCT
GAAATGGCTATCTCTTCTCCGCTGCTGGAAGATATCGACCTGTCTGGCGCGCGCGGCGTG
CTGGTTAACATCACGGCGGGCTTCGACCTGCGTCTGGATGAGTTCGAAACGGTAGGTAAC
ACCATCCGTGCATTTGCTTCCGACAACGCGACTGTGGTTATCGGTACTTCTCTTGACCCG
GATATGAATGACGAGCTGCGCGTAACCGTTGTTGCGACAGGTATCGGCATGGACAAACGT
CCTGAAATCACTCTGGTGACCAATAAGCAGGTTCAGCAGCCAGTGATGGATCGCTACCAG
CAGCATGGGATGGCTCCGCTGACCCAGGAGCAGAAGCCGGTTGCTAAAGTCGTGAATGAC
AATGCGCCGCAAACTGCGAAAGAGCCGGATTATCTGGATATCCCAGCATTCCTGCGTAAG
CAAGCTGATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:383
Protein Molecular Weight:42347
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Acetylornithine deacetylase
MKNKLPPFIEIYRALIATPSISATEEALDQSNADLITLLADWFKDLGFNVEVQPVPGTRN
KFNMLASIGQGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFI
LDALRDVDVTKLKKPLYILATADEETSMAGARYFAETTALRPDCAIIGEPTSLQPVRAHK
GHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLN
LGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVDELHP
PIPGYECPPNHQLVEVVEKLLGAKTEVVNYCTEAPFIQTLCPTLVLGPGSINQAHQPDEY
LETRFIKPTRELITQVIHHFCWH
References
External Links:
ResourceLink
Uniprot ID:P23908
Uniprot Name:ARGE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674323
Ecogene ID:EG11286
Ecocyc:EG11286
ColiBase:b3957
Kegg Gene:b3957
EchoBASE ID:EB1263
CCDB:ARGE_ECOLI
BacMap:16131795
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
  • Boyen, A., Charlier, D., Charlier, J., Sakanyan, V., Mett, I., Glansdorff, N. (1992). "Acetylornithine deacetylase, succinyldiaminopimelate desuccinylase and carboxypeptidase G2 are evolutionarily related." Gene 116:1-6. Pubmed: 1628835
  • Charlier, D., Piette, J., Glansdorff, N. (1982). "IS3 can function as a mobile promoter in E. coli." Nucleic Acids Res 10:5935-5948. Pubmed: 6292860
  • 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
  • Javid-Majd, F., Blanchard, J. S. (2000). "Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase." Biochemistry 39:1285-1293. Pubmed: 10684608
  • Meinnel, T., Schmitt, E., Mechulam, Y., Blanquet, S. (1992). "Structural and biochemical characterization of the Escherichia coli argE gene product." J Bacteriol 174:2323-2331. Pubmed: 1551850
  • Piette, J., Cunin, R., Boyen, A., Charlier, D., Crabeel, M., Van Vliet, F., Glansdorff, N., Squires, C., Squires, C. L. (1982). "The regulatory region of the divergent argECBH operon in Escherichia coli K-12." Nucleic Acids Res 10:8031-8048. Pubmed: 6761650