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 ...
14-416
0e+00
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: 552.32 E-value: 0e+00
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
14-416
0e+00
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: 552.32 E-value: 0e+00
selenoneine synthase SenA; Selenoneine is the selenium analog of ergothioneine, a ...
12-416
9.43e-114
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: 337.93 E-value: 9.43e-114
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
223-417
2.56e-24
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: 101.04 E-value: 2.56e-24
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
14-416
0e+00
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: 552.32 E-value: 0e+00
selenoneine synthase SenA; Selenoneine is the selenium analog of ergothioneine, a ...
12-416
9.43e-114
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: 337.93 E-value: 9.43e-114
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
223-417
2.56e-24
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: 101.04 E-value: 2.56e-24
DinB superfamily; The DinB family are an uncharacterized family of potential enzymes. The ...
17-149
2.97e-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: 52.08 E-value: 2.97e-08
EgtB-related enzyme signature domain; This model represents a signature C-terminal region of a ...
381-414
1.00e-04
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: 39.67 E-value: 1.00e-04
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
mapped to the query sequence.
Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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