Protein Family Models

The DinB family are an uncharacterised family of potential enzymes. The structure of these proteins is composed of a four helix bundle [1]. [1]. 20208147. The structure of DinB from Geobacillus stearothermophilus: a. representative of a unique four-helix-bundle superfamily.. Cooper DR, Grelewska K, Kim CY, Joachimiak A, Derewenda ZS;. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010;66:219-224. (from Pfam)

Date:

2024-04-03

This domain is found in eukaryotic proteins [1] required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD) [2]. 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 [3]. FGE is localised to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesised sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilised 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 oxidised 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 [4]. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase [5,6]. [1]. 14563551. The human SUMF1 gene, required for posttranslational sulfatase. modification, defines a new gene family which is conserved from. pro- to eukaryotes.. Landgrebe J, Dierks T, Schmidt B, von Figura K;. Gene 2003;316:47-56.. [2]. 15146462. Molecular and functional analysis of SUMF1 mutations in multiple. sulfatase deficiency.. Cosma MP, Pepe S, Parenti G, Settem. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-04-03

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).

Gene:

egtB

Date:

2021-04-27

ergothioneine biosynthesis protein EgtB catalyzes the oxidative sulfurization of hercynine (N-alpha,N-alpha,N-alpha-trimethyl-L-histidine) into hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide, a step in the biosynthetic pathway of ergothioneine

Date:

2018-02-05