Isoaspartyl dipeptidase
Details
- Name
- Isoaspartyl dipeptidase
- Kind
- protein
- Synonyms
- 3.4.19.-
- yjiF
- Gene Name
- iadA
- UniProtKB Entry
- P39377Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0016562|Isoaspartyl dipeptidase MIDYTAAGFTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQIL CPGFIDQHVHLIGGGGEAGPTTRTPEVALSRLTEAGVTSVVGLLGTDSISRHPESLLAKT RALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGVKCAISDHRSAAPDVYHLAN MAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQ ALEFARKGGTIDITSSIDEPVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLT HIGVAGFETLLETVQVLVKDYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMT PELRIEQVYARGKLMVKDGKACVKGTFETA
- Number of residues
- 390
- Molecular Weight
- 41083.515
- Theoretical pI
- 4.89
- GO Classification
- Functionsbeta-aspartyl-peptidase activity / hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds / metallopeptidase activity / zinc ion bindingComponentscytoplasm / cytosol
- General Function
- Catalyzes the hydrolytic cleavage of a subset of L-isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu.
- Specific Function
- beta-aspartyl-peptidase activity
- Pfam Domain Function
- Amidohydro_1 (PF01979)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0016563|Isoaspartyl dipeptidase (iadA) ATGATTGATTATACCGCAGCCGGTTTTACCCTGCTGCAGGGAGCGCATTTGTATGCGCCG GAAGATCGGGGAATTTGCGATGTCCTCGTCGCTAACGGCAAAATTATCGCCGTTGCCAGC AATATCCCTTCTGACATTGTACCGAACTGCACGGTTGTCGATCTCAGTGGGCAGATCCTC TGCCCAGGTTTTATTGATCAACACGTCCATTTGATTGGCGGTGGCGGCGAAGCAGGTCCC ACGACGCGCACGCCGGAAGTGGCGCTAAGTCGCCTGACGGAAGCGGGCGTCACGTCAGTG GTTGGTCTGCTGGGCACCGACTCTATCTCTCGCCACCCGGAATCCCTGCTCGCCAAGACC CGTGCGCTCAATGAAGAAGGCATCAGCGCCTGGATGCTGACCGGCGCTTATCATGTCCCT TCCCGCACCATTACGGGTTCCGTGGAAAAAGACGTGGCGATTATCGATCGTGTGATTGGC GTGAAATGCGCCATCTCTGATCACCGTTCTGCCGCACCGGACGTTTATCACCTGGCCAAT ATGGCGGCAGAATCCCGCGTTGGCGGTTTGCTCGGCGGTAAACCTGGCGTCACCGTGTTC CACATGGGCGACAGTAAAAAGGCGTTACAGCCTATTTATGACCTGCTGGAAAACTGCGAT GTGCCGATCAGCAAGCTGCTGCCGACCCACGTTAACCGCAACGTACCGTTGTTTGAGCAG GCGCTGGAGTTCGCGCGCAAAGGCGGCACCATCGATATCACCAGCAGCATTGACGAACCG GTCGCCCCTGCCGAAGGTATTGCCCGCGCCGTTCAGGCGGGTATTCCGCTGGCACGCGTC ACCCTCAGCTCCGACGGCAACGGTAGCCAGCCGTTCTTCGATGACGAAGGGAATTTAACC CATATCGGTGTTGCCGGTTTTGAAACGTTGCTGGAAACCGTGCAGGTGCTGGTCAAAGAC TATGATTTCAGTATCAGCGATGCCCTGCGCCCGCTCACCAGTAGCGTAGCCGGTTTCCTT AACCTGACCGGGAAAGGCGAAATTCTGCCAGGCAATGATGCTGACTTGCTGGTCATGACG CCAGAACTGCGCATTGAGCAGGTATACGCTCGCGGCAAACTGATGGTCAAAGACGGCAAA GCCTGCGTGAAAGGAACGTTTGAAACGGCTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P39377 UniProtKB Entry Name IADA_ECOLI GenBank Protein ID 640031 GenBank Gene ID U15029 PDB ID(s) 1ONW, 1ONX, 1PO9, 1POJ, 1POK, 1YBQ, 2AQO, 2AQV KEGG ID ecj:JW4291 NCBI Gene ID 948853 - General References
- Gary JD, Clarke S: Purification and characterization of an isoaspartyl dipeptidase from Escherichia coli. J Biol Chem. 1995 Feb 24;270(8):4076-87. [Article]
- Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [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]
- Haley EE: Purification and properties of a beta-aspartyl peptidase from Escherichia coli. J Biol Chem. 1968 Nov 10;243(21):5748-52. [Article]
- Thoden JB, Marti-Arbona R, Raushel FM, Holden HM: High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 2003 May 6;42(17):4874-82. [Article]
- Jozic D, Kaiser JT, Huber R, Bode W, Maskos K: X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases. J Mol Biol. 2003 Sep 5;332(1):243-56. [Article]
- Marti-Arbona R, Fresquet V, Thoden JB, Davis ML, Holden HM, Raushel FM: Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 2005 May 17;44(19):7115-24. [Article]
- Marti-Arbona R, Thoden JB, Holden HM, Raushel FM: Functional significance of Glu-77 and Tyr-137 within the active site of isoaspartyl dipeptidase. Bioorg Chem. 2005 Dec;33(6):448-58. Epub 2005 Nov 11. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details (5r)-5-Amino-6-Hydroxyhexylcarbamic Acid experimental unknown target Details Lysine Nz-Carboxylic Acid experimental unknown target Details