Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones].

Sulfatase-modifying factor enzyme 1. This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.

Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.

BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.

Structureof PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5HHA_B Structure of PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]

Formylglycinegenerating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_B Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_C Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_D Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)],6MUJ_E Formylglycine generating enzyme bound to copper [Streptomyces coelicolor A3(2)]

wild-typeFormylglycine generating enzyme reacted with iodoacetamide [Homo sapiens]

ChainX, Sulfatase modifying factor 1 [Homo sapiens],2AIJ_X Chain X, Sulfatase modifying factor 1 [Homo sapiens],2AIK_X Chain X, Sulfatase modifying factor 1 [Homo sapiens],2HI8_X Chain X, Sulfatase-modifying factor 1 [Homo sapiens],2HIB_X Chain X, Sulfatase-modifying factor 1 [Homo sapiens]

ChainX, Sulfatase modifying factor 1 [Homo sapiens]

Formylglycine-generating enzyme OS=Bos taurus OX=9913 GN=SUMF1 PE=2 SV=1

Formylglycine-generating enzyme OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=SCO7548 PE=1 SV=1

Formylglycine-generating enzyme OS=Mus musculus OX=10090 GN=Sumf1 PE=1 SV=2

Formylglycine-generating enzyme OS=Homo sapiens OX=9606 GN=SUMF1 PE=1 SV=3

Formylglycine-generating enzyme OS=Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9) OX=471852 GN=Tcur_4811 PE=1 SV=1