D-lyxose/D-mannose family sugar isomerase is a cupin-domain containing protein similar to Serratia proteamaculans D-lyxose isomerase that produces D-lyxose and D-mannose
D-lyxose isomerase; Members of this family of sugar isomerases belong to the cupin superfamily. ...
1-224
6.42e-150
D-lyxose isomerase; Members of this family of sugar isomerases belong to the cupin superfamily. The enzyme from Cohnella laevoribosii has been shown to be specific for D-lyxose, L-ribose, and D-mannose. E. coli sugar isomerase (EcSI) has been structurally and functionally characterized and shows a preference for D-lyxose and D-mannose.
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Pssm-ID: 429437 Cd Length: 223 Bit Score: 415.80 E-value: 6.42e-150
D-lyxose isomerase; Members of this family of sugar isomerases belong to the cupin superfamily. ...
1-224
6.42e-150
D-lyxose isomerase; Members of this family of sugar isomerases belong to the cupin superfamily. The enzyme from Cohnella laevoribosii has been shown to be specific for D-lyxose, L-ribose, and D-mannose. E. coli sugar isomerase (EcSI) has been structurally and functionally characterized and shows a preference for D-lyxose and D-mannose.
Pssm-ID: 429437 Cd Length: 223 Bit Score: 415.80 E-value: 6.42e-150
Escherichia coli sugar isomerase (EcSI), cupin domain; This family includes a sugar isomerase ...
2-201
2.39e-126
Escherichia coli sugar isomerase (EcSI), cupin domain; This family includes a sugar isomerase homologous to pathogenic Escherichia coli O157 z5688 D-lyxose isomerase (EcSI or Z5688) which has an active site highly similar to YdaE from the sigma B regulon of Bacillus subtilis. Extensive substrate screening has revealed that EcSI is capable of acting on D-lyxose and D-mannose. Studies show that overexpression of EcSI enables cell growth on D-lyxose as the sole carbon source. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.
Pssm-ID: 380443 Cd Length: 199 Bit Score: 355.33 E-value: 2.39e-126
D-lyxose isomerase; Members of this family of sugar isomerases belong to the cupin superfamily. ...
1-224
6.42e-150
D-lyxose isomerase; Members of this family of sugar isomerases belong to the cupin superfamily. The enzyme from Cohnella laevoribosii has been shown to be specific for D-lyxose, L-ribose, and D-mannose. E. coli sugar isomerase (EcSI) has been structurally and functionally characterized and shows a preference for D-lyxose and D-mannose.
Pssm-ID: 429437 Cd Length: 223 Bit Score: 415.80 E-value: 6.42e-150
Escherichia coli sugar isomerase (EcSI), cupin domain; This family includes a sugar isomerase ...
2-201
2.39e-126
Escherichia coli sugar isomerase (EcSI), cupin domain; This family includes a sugar isomerase homologous to pathogenic Escherichia coli O157 z5688 D-lyxose isomerase (EcSI or Z5688) which has an active site highly similar to YdaE from the sigma B regulon of Bacillus subtilis. Extensive substrate screening has revealed that EcSI is capable of acting on D-lyxose and D-mannose. Studies show that overexpression of EcSI enables cell growth on D-lyxose as the sole carbon source. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.
Pssm-ID: 380443 Cd Length: 199 Bit Score: 355.33 E-value: 2.39e-126
sugar isomerase such as lyxose isomerase, cupin domain; This family includes D-lyxose ...
89-189
5.06e-53
sugar isomerase such as lyxose isomerase, cupin domain; This family includes D-lyxose isomerase (D-LI; EC 5.3.1.15) homologous to YdaE from the sigma B regulon of Bacillus subtilis and to pathogenic Escherichia coli O157 z5688 D-lyxose isomerase (EcSI or Z5688), both having highly similar active sites. YdaE may have a synergistic role with ydaD, an NAD(P)-dependent alcohol dehydrogenase, in the adaptation to environment stresses, while EcSI has D-lyxose/D-mannose activity. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.
Pssm-ID: 380402 Cd Length: 100 Bit Score: 165.87 E-value: 5.06e-53
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
131-179
3.18e-05
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.
Pssm-ID: 380358 [Multi-domain] Cd Length: 83 Bit Score: 40.96 E-value: 3.18e-05
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.
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