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. ...
1-223
1.09e-163
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: 450.47 E-value: 1.09e-163
D-lyxose isomerase; Members of this family of sugar isomerases belong to the cupin superfamily. ...
1-223
1.09e-163
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: 450.47 E-value: 1.09e-163
Escherichia coli sugar isomerase (EcSI), cupin domain; This family includes a sugar isomerase ...
2-200
4.81e-140
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: 390.00 E-value: 4.81e-140
D-lyxose isomerase; Members of this family of sugar isomerases belong to the cupin superfamily. ...
1-223
1.09e-163
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: 450.47 E-value: 1.09e-163
Escherichia coli sugar isomerase (EcSI), cupin domain; This family includes a sugar isomerase ...
2-200
4.81e-140
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: 390.00 E-value: 4.81e-140
sugar isomerase such as lyxose isomerase, cupin domain; This family includes D-lyxose ...
88-187
5.66e-23
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: 89.22 E-value: 5.66e-23
D-lyxose isomerase YdaE, cupin domain; This family includes D-lyxose isomerase (D-LI; EC 5.3.1. ...
43-172
5.01e-09
D-lyxose isomerase YdaE, 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, a protein with an active site that is highly similar to the E. coli O157 z5688 D-lyxose isomerase. YdaE may have a synergistic role with ydaD, an NAD(P)-dependent alcohol dehydrogenase, in the adaptation to environment stresses; YdaD may be active against the ketose sugar produced by YdaE and function in providing resistance to oxidative stress through the production of reducing equivalents in the form of NAD(P)H. YdaE forms a cupin-type beta-barrel, with two alpha helices at the N-terminus. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.
Pssm-ID: 380442 Cd Length: 160 Bit Score: 53.37 E-value: 5.01e-09
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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