AGE (N-acylglucosamine 2-epimerase) family epimerase/isomerase with the common scaffold, alpha6/alpha6-barrel; similar to sulfoquinovose isomerase and D-mannose isomerase
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
37-391
4.45e-149
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of eukaryotic and bacterial N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase) enzymes (EC:5.1.3.8) approximately 500 residues long. This converts N-acyl-D-glucosamine to N-acyl-D-mannosamine.
:
Pssm-ID: 399891 Cd Length: 347 Bit Score: 426.43 E-value: 4.45e-149
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
37-391
4.45e-149
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of eukaryotic and bacterial N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase) enzymes (EC:5.1.3.8) approximately 500 residues long. This converts N-acyl-D-glucosamine to N-acyl-D-mannosamine.
Pssm-ID: 399891 Cd Length: 347 Bit Score: 426.43 E-value: 4.45e-149
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
24-395
1.54e-65
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.
Pssm-ID: 238153 Cd Length: 384 Bit Score: 213.76 E-value: 1.54e-65
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
37-391
4.45e-149
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of eukaryotic and bacterial N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase) enzymes (EC:5.1.3.8) approximately 500 residues long. This converts N-acyl-D-glucosamine to N-acyl-D-mannosamine.
Pssm-ID: 399891 Cd Length: 347 Bit Score: 426.43 E-value: 4.45e-149
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
24-395
1.54e-65
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.
Pssm-ID: 238153 Cd Length: 384 Bit Score: 213.76 E-value: 1.54e-65
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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This image shows a graphical summary of conserved domains identified on the query sequence.
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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,
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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,
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specific hits meet or exceed a domain-specific e-value threshold
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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
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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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