Annotations: 6O6L

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	UNK_F_TYPE	e6o6lA2	A: alpha bundles	X: YfiT-like putative metal-dependent hydrolases (From Topology)	H: YfiT-like putative metal-dependent hydrolases (From Topology)	T: YfiT-like putative metal-dependent hydrolases	F: UNK_F_TYPE	ECOD (1.6)
A	FGE-sulfatase	e6o6lA1	A: a+b complex topology	X: C-type lectin-like (From Homology)	H: C-type lectin-like	T: Sulfatase-modifying factor-like	F: FGE-sulfatase	ECOD (1.6)
C	UNK_F_TYPE	e6o6lC1	A: alpha bundles	X: YfiT-like putative metal-dependent hydrolases (From Topology)	H: YfiT-like putative metal-dependent hydrolases (From Topology)	T: YfiT-like putative metal-dependent hydrolases	F: UNK_F_TYPE	ECOD (1.6)
C	FGE-sulfatase	e6o6lC2	A: a+b complex topology	X: C-type lectin-like (From Homology)	H: C-type lectin-like	T: Sulfatase-modifying factor-like	F: FGE-sulfatase	ECOD (1.6)
D	UNK_F_TYPE	e6o6lD1	A: alpha bundles	X: YfiT-like putative metal-dependent hydrolases (From Topology)	H: YfiT-like putative metal-dependent hydrolases (From Topology)	T: YfiT-like putative metal-dependent hydrolases	F: UNK_F_TYPE	ECOD (1.6)
D	FGE-sulfatase	e6o6lD2	A: a+b complex topology	X: C-type lectin-like (From Homology)	H: C-type lectin-like	T: Sulfatase-modifying factor-like	F: FGE-sulfatase	ECOD (1.6)
B	UNK_F_TYPE	e6o6lB2	A: alpha bundles	X: YfiT-like putative metal-dependent hydrolases (From Topology)	H: YfiT-like putative metal-dependent hydrolases (From Topology)	T: YfiT-like putative metal-dependent hydrolases	F: UNK_F_TYPE	ECOD (1.6)
B	FGE-sulfatase	e6o6lB1	A: a+b complex topology	X: C-type lectin-like (From Homology)	H: C-type lectin-like	T: Sulfatase-modifying factor-like	F: FGE-sulfatase	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF03781	Sulfatase-modifying factor enzyme 1 (FGE-sulfatase)	Sulfatase-modifying factor enzyme 1	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 FG ...	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].	Domain
A, B, C, D	PF12867	DinB superfamily (DinB_2)	DinB superfamily	The DinB family are an uncharacterised family of potential enzymes. The structure of these proteins is composed of a four helix bundle [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	EgtB (Cabther)	cation binding ion binding binding metal ion binding small molecule binding	amino-acid betaine biosynthetic process oxoacid metabolic process small molecule biosynthetic process sulfur amino acid metabolic process modified amino acid biosynthetic process carboxylic acid metabolic process modified amino acid metabolic process organic acid metabolic process organic acid biosynthetic process ergothioneine metabolic process amino-acid betaine metabolic process carboxylic acid biosynthetic process sulfur compound biosynthetic process biosynthetic process modified histidine biosynthetic process amino-acid betaine biosynthetic process oxoacid metabolic process small molecule biosynthetic process sulfur amino acid metabolic process modified amino acid biosynthetic process carboxylic acid metabolic process modified amino acid metabolic process organic acid metabolic process organic acid biosynthetic process ergothioneine metabolic process amino-acid betaine metabolic process carboxylic acid biosynthetic process sulfur compound biosynthetic process biosynthetic process modified histidine biosynthetic process ergothioneine biosynthetic process sulfur compound metabolic process metabolic process cellular process small molecule metabolic process modified histidine metabolic process sulfur amino acid biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR042095	Sulfatase-modifying factor enzyme superfamily	Homologous Superfamily
A, B, C, D	IPR005532	Sulfatase-modifying factor enzyme	Domain
A, B, C, D	IPR024775	DinB-like domain	Domain
A, B, C, D	IPR017806	Ergothioneine biosynthesis protein EgtB	Family
A, B, C, D	IPR016187	C-type lectin fold	Homologous Superfamily
A, B, C, D	IPR034660	DinB/YfiT-like putative metalloenzymes	Homologous Superfamily
A, B, C, D	IPR051043	Sulfatase Modifying Factor and Kinase	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.