InterPro domain: IPR042095

This superfamily represents a domain is found in sulfatase-modifying factors (SUMFs) [ 1 ] and Chlamydia serine/threonine-protein kinase pkn1 [ 2 ]. It is also found in iron(II)-dependent oxidoreductase from Mycobacterium [ 3 , 4 ].

The structure of this domain is homologous to the complex alpha/beta topology found in sulfatase-modifying factors (SUMF1). SUMF1 is a paralogue of oxoalanine-generating enzyme, also called C(alpha)-formylglycine generating enzyme (FGE). SUMF1 converts newly synthesized inactive sulfatases to their active form by modifying an active site cysteine residue to oxoalanine. Sulfatases are essential for the degradation of sulfate esters, whose catalytic activity is dependent upon an oxoalanine residue [ 5 ]. Defects in SUMF1 or FGE cause multiple sulfatase deficiency (MSD), which leads to the impairment of all sulfatases and to the accumulation of glycoaminoglycans or sulfolipids, causing early infant death [ 6 , 7 , 8 ] Known substrates for SUMF1 are: N-acetylgalactosamine-6-sulfate sulfatase (GALNS), arylsulfatase A (ARSA), steroid sulfatase (STS) and arylsulfatase E (ARSE). SUMF1 occurs in the endoplasmic reticulum or its lumen.

1. The human SUMF1 gene, required for posttranslational sulfatase modification, defines a new gene family which is conserved from pro- to eukaryotes. Gene 316, 47-56
2. Identification of two eukaryote-like serine/threonine kinases encoded by Chlamydia trachomatis serovar L2 and characterization of interacting partners of Pkn1. J. Am. Chem. Soc. 71, 5772-84
3. In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 132, 6632-3
4. Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes. null 101, 5646-51
5. De novo calcium/sulfur SAD phasing of the human formylglycine-generating enzyme using in-house data. Acta Crystallogr. D Biol. Crystallogr. 61, 1057-66
6. SUMF1 enhances sulfatase activities in vivo in five sulfatase deficiencies. Biochem. J. 403, 305-12
7. Sulfatases and human disease. Hum. Mol. Genet. 6, 355-79
8. Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship. Infect. Immun. 14, 3203-17