HMM Summary Page: TIGR01975

Functionbeta-aspartyl peptidase
Gene SymboliadA
Trusted Cutoff331.25
Domain Trusted Cutoff331.25
Noise Cutoff101.80
Domain Noise Cutoff101.80
Isology Typeequivalog
EC Number3.4.19.5
HMM Length389
Mainrole CategoryProtein fate
Subrole CategoryDegradation of proteins, peptides, and glycopeptides
Gene Ontology TermGO:0006508: proteolysis biological_process
GO:0008798: beta-aspartyl-peptidase activity molecular_function
AuthorHaft DH
Entry DateSep 3 2003 4:52PM
Last ModifiedFeb 14 2011 3:27PM
CommentThe L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This HMM describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases.
ReferencesDR EXPERIMENTAL; SP|P39377; Escherichia coli RM 7876157 RT Purification and characterization of an isoaspartyl dipeptidase from Escherichia coli. RA Gary JD, Clarke S. RL J Biol Chem. 1995 Feb 24;270(8):4076-87.