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FGE

Function

Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:25931126, PubMed:16368756, PubMed:21224894). 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile (PubMed:12757706, PubMed:15657036, PubMed:15907468, PubMed:25931126, PubMed:16368756). Known substrates include GALNS, ARSA, STS and ARSE (PubMed:12757706, PubMed:15907468, PubMed:15657036).

Involvement in disease

Multiple sulfatase deficiency

MSD

A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay.

None

The disease is caused by variants affecting the gene represented in this entry. SUMF1 mutations result in defective post-translational modification of sulfatases.

Pathway

Protein modification; sulfatase oxidation.

Post-translational modifications

N-glycosylated. Contains high-mannose-type oligosaccharides.

Sequence similarities

Belongs to the sulfatase-modifying factor family.

Tissue specificity

Ubiquitous. Highly expressed in kidney, pancreas and liver. Detected at lower levels in leukocytes, lung, placenta, small intestine, skeletal muscle and heart.

Cellular localization

  • Endoplasmic reticulum lumen

Alternative names

  • Formylglycine-generating enzyme
  • FGE
  • C-alpha-formylglycine-generating enzyme 1
  • Sulfatase-modifying factor 1
  • UNQ3037/PRO9852
  • PSEC0152
  • SUMF1

Target type

Proteins

Molecular weight

40556Da