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
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
7-422
2.18e-139
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: 404.40 E-value: 2.18e-139
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
7-422
2.18e-139
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: 404.40 E-value: 2.18e-139
selenoneine synthase SenA; Selenoneine is the selenium analog of ergothioneine, a ...
3-422
4.58e-90
selenoneine synthase SenA; Selenoneine is the selenium analog of ergothioneine, a sulfur-containing derivative of a hercynine, which derives from histidine by trimethylation of its amino group. SenA, a homolog of ergothioneine biosynthesis protein EgtB, completes selenoneine biosynthesis in a pathway that also requires a SelD protein to prepare selenophosphate, EgtD to prepare hercynine, and the selenosugar-producing glycosyltransferase SenB (TIGR04348). SenA catalyzes selenium-carbon bond formation between hercynine and selenosugar to produce selenoneine. Other enzymes that create carbon-selenium bonds include SelA, involved in selenocysteine biosynthesis, SelU, involved in selenouridine biosynthesis, and SbtM, a radical SAM enzyme involved in post-translational modification of the RiPP precursor SbtA (see PMID:34730336).
Pssm-ID: 469092 [Multi-domain] Cd Length: 384 Bit Score: 277.84 E-value: 4.58e-90
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
163-423
2.76e-66
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: 212.36 E-value: 2.76e-66
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
7-422
2.18e-139
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: 404.40 E-value: 2.18e-139
selenoneine synthase SenA; Selenoneine is the selenium analog of ergothioneine, a ...
3-422
4.58e-90
selenoneine synthase SenA; Selenoneine is the selenium analog of ergothioneine, a sulfur-containing derivative of a hercynine, which derives from histidine by trimethylation of its amino group. SenA, a homolog of ergothioneine biosynthesis protein EgtB, completes selenoneine biosynthesis in a pathway that also requires a SelD protein to prepare selenophosphate, EgtD to prepare hercynine, and the selenosugar-producing glycosyltransferase SenB (TIGR04348). SenA catalyzes selenium-carbon bond formation between hercynine and selenosugar to produce selenoneine. Other enzymes that create carbon-selenium bonds include SelA, involved in selenocysteine biosynthesis, SelU, involved in selenouridine biosynthesis, and SbtM, a radical SAM enzyme involved in post-translational modification of the RiPP precursor SbtA (see PMID:34730336).
Pssm-ID: 469092 [Multi-domain] Cd Length: 384 Bit Score: 277.84 E-value: 4.58e-90
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
163-423
2.76e-66
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: 212.36 E-value: 2.76e-66
5-histidylcysteine sulfoxide synthase; Ovothiol A is N1-methyl-4-mercaptohistidine. In the ...
125-422
2.65e-37
5-histidylcysteine sulfoxide synthase; Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes the 5-histidylcysteine sulfoxide synthase domain, a homolog of the ergothioneine biosynthesis protein EgtB. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 275140 [Multi-domain] Cd Length: 442 Bit Score: 140.88 E-value: 2.65e-37
EgtB-related enzyme signature domain; This model represents a signature C-terminal region of a ...
373-420
1.38e-10
EgtB-related enzyme signature domain; This model represents a signature C-terminal region of a distinct clade in the EgtB subfamily, other members of which participate in ergothioneine biosynthesis
Pssm-ID: 275166 [Multi-domain] Cd Length: 50 Bit Score: 56.24 E-value: 1.38e-10
DinB superfamily; The DinB family are an uncharacterized family of potential enzymes. The ...
10-137
4.67e-08
DinB superfamily; The DinB family are an uncharacterized family of potential enzymes. The structure of these proteins is composed of a four helix bundle.
Pssm-ID: 463733 Cd Length: 128 Bit Score: 51.31 E-value: 4.67e-08
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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