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Aspartyl Dipeptidase

Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Biochemical function: dipeptidase activity
Biological process: proteolysis
Cellular component: cytoplasm

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EC 3.4.13.21: Dipeptidase E

Reaction catalysed:
Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.
Alternative Name(s):
  • Aspartyl dipeptidase
  • PepE gene product (Salmonella typhimurium)
  • Peptidase E

GO terms

Biochemical function:
Biological process:
Cellular component:

Sequence family

Pfam Protein family (Pfam)
PF03575
Domain description: Peptidase family S51
Occurring in:
  1. Peptidase E
The deposited structure of PDB entry 1fy2 contains 1 copy of Pfam domain PF03575 (Peptidase family S51) in Peptidase E. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR005320
Domain description: Peptidase S51
Occurring in:
  1. Peptidase E
IPR029062
Domain description: Class I glutamine amidotransferase-like
Occurring in:
  1. Peptidase E
IPR023172
Domain description: Peptidase S51, dipeptidase E
Occurring in:
  1. Peptidase E

Structure domain

CATH CATH domain
3.40.50.880
Class: Alpha Beta
Architecture: 3-Layer(aba) Sandwich
Topology: Rossmann fold
Homology: Rossmann fold
Occurring in:
  1. Peptidase E
The deposited structure of PDB entry 1fy2 contains 1 copy of CATH domain 3.40.50.880 (Rossmann fold) in Peptidase E. Showing 1 copy in chain A.
SCOP SCOP annotation
52331
Class: Alpha and beta proteins (a/b)
Fold: Flavodoxin-like
Superfamily: Class I glutamine amidotransferase-like
Occurring in:
  1. Peptidase E
The deposited structure of PDB entry 1fy2 contains 1 copy of SCOP domain 52331 (Aspartyl dipeptidase PepE) in Peptidase E. Showing 1 copy in chain A.

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