SUMF1/EgtB/PvdO family nonheme iron enzyme [Rhizobium leguminosarum]
Protein Classification
formylglycine-generating enzyme family protein( domain architecture ID 581145)
formylglycine-generating enzyme family protein similar to human sulfatase-modifying factor 1 (SUMF1), which oxidizes a cysteine residue in the substrate sulfatase, to an active site 3-oxoalanine residue, also called C(alpha)-formylglycine
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| FGE-sulfatase super family | cl23855 | Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ... |
12-224 | 4.39e-15 | |||||
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. The actual alignment was detected with superfamily member pfam03781: Pssm-ID: 474083 [Multi-domain] Cd Length: 259 Bit Score: 72.15 E-value: 4.39e-15
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| Name | Accession | Description | Interval | E-value | |||||
| FGE-sulfatase | pfam03781 | Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ... |
12-224 | 4.39e-15 | |||||
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. Pssm-ID: 397722 [Multi-domain] Cd Length: 259 Bit Score: 72.15 E-value: 4.39e-15
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| YfmG | COG1262 | Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ... |
12-224 | 1.90e-14 | |||||
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440874 [Multi-domain] Cd Length: 238 Bit Score: 70.03 E-value: 1.90e-14
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| egtB_TIGR03440 | TIGR03440 | ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ... |
64-166 | 4.61e-04 | |||||
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of the ergothioneine biosynthesis, as found in numerous Actinobacteria. Characterized homologs to this family include a formylglycine-generating enzyme that serves as a maturase for an aerobic sulfatase (cf. the radical SAM enzymes that serve as anaerobic sulfatase maturases). [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs] Pssm-ID: 274581 [Multi-domain] Cd Length: 406 Bit Score: 40.77 E-value: 4.61e-04
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| Name | Accession | Description | Interval | E-value | |||||
| FGE-sulfatase | pfam03781 | Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ... |
12-224 | 4.39e-15 | |||||
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. Pssm-ID: 397722 [Multi-domain] Cd Length: 259 Bit Score: 72.15 E-value: 4.39e-15
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| YfmG | COG1262 | Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ... |
12-224 | 1.90e-14 | |||||
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440874 [Multi-domain] Cd Length: 238 Bit Score: 70.03 E-value: 1.90e-14
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| egtB_TIGR03440 | TIGR03440 | ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ... |
64-166 | 4.61e-04 | |||||
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of the ergothioneine biosynthesis, as found in numerous Actinobacteria. Characterized homologs to this family include a formylglycine-generating enzyme that serves as a maturase for an aerobic sulfatase (cf. the radical SAM enzymes that serve as anaerobic sulfatase maturases). [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs] Pssm-ID: 274581 [Multi-domain] Cd Length: 406 Bit Score: 40.77 E-value: 4.61e-04
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