› › Function and Biology

Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria

Source organism: Elizabethkingia miricola
Biochemical function: hydrolase activity
Biological process: proteolysis
Cellular component: periplasmic space

Quick links

EC 3.5.1.26: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase

Reaction catalysed:
N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-D-glucosaminylamine + L-aspartate
Systematic name:
N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Alternative Name(s):
  • 4-N-(beta-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
  • Aspartylglucosaminidase
  • Aspartylglucosylaminase
  • Aspartylglucosylamine deaspartylase
  • Aspartylglucosylaminidase
  • Aspartylglycosylamine amidohydrolase
  • Beta-aspartylglucosylamine amidohydrolase
  • Glucosylamidase
  • Glycosylasparaginase
  • N-aspartyl-beta-glucosaminidase

GO terms

Sequence family

Pfam Protein family (Pfam)
PF01112
Domain description: Asparaginase
Occurring in:
  1. N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase
The deposited structure of PDB entry 4r4y contains 2 copies of Pfam domain PF01112 (Asparaginase) in N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR000246
Domain description: Peptidase T2, asparaginase 2
Occurring in:
  1. N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase
IPR029055
Domain description: Nucleophile aminohydrolases, N-terminal
Occurring in:
  1. N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase

Quick links