AGE (N-acylglucosamine 2-epimerase) family epimerase/isomerase with the common scaffold, alpha6/alpha6-barrel; similar to N-acylglucosamine 2-epimerase
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
4-397
2.05e-145
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: 418.69 E-value: 2.05e-145
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
4-397
2.05e-145
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: 418.69 E-value: 2.05e-145
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
37-375
6.40e-39
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: 142.92 E-value: 6.40e-39
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
4-397
2.05e-145
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: 418.69 E-value: 2.05e-145
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
37-375
6.40e-39
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: 142.92 E-value: 6.40e-39
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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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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