riboflavin synthase catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil, the last step of riboflavin biosynthesis
Riboflavin synthase alpha chain [Coenzyme transport and metabolism]; Riboflavin synthase alpha ...
1-196
3.17e-99
Riboflavin synthase alpha chain [Coenzyme transport and metabolism]; Riboflavin synthase alpha chain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
:
Pssm-ID: 440076 Cd Length: 198 Bit Score: 285.78 E-value: 3.17e-99
Riboflavin synthase alpha chain [Coenzyme transport and metabolism]; Riboflavin synthase alpha ...
1-196
3.17e-99
Riboflavin synthase alpha chain [Coenzyme transport and metabolism]; Riboflavin synthase alpha chain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 440076 Cd Length: 198 Bit Score: 285.78 E-value: 3.17e-99
Riboflavin synthase and similar proteins; Riboflavin synthase catalyzes the dismutation of two ...
1-185
1.57e-92
Riboflavin synthase and similar proteins; Riboflavin synthase catalyzes the dismutation of two molecules of 6,7-dimethyl-8-(1'-D-ribityl)-lumazine (DMRL) to yield riboflavin (vitamin B12) and 4-ribitylamino-5-amino-2,6-dihydroxypyrimidine (RAADP). Riboflavin synthase is a homotrimer and the catalysis does not require any cofactors. Active sites are located between pairs of monomers, but only one active site catalyzes a reaction, the other two sites are inactive. Humans do not produce riboflavin synthase, and thus it is a good target for antimicrobial agents. This family also include lumazine protein (LumP) from bioluminescent bacteria. LumP serves as an optical transponder in bioluminescence emission.
Pssm-ID: 293928 Cd Length: 185 Bit Score: 268.49 E-value: 1.57e-92
riboflavin synthase, alpha subunit; This protein family consists almost entirely of two ...
1-193
5.29e-62
riboflavin synthase, alpha subunit; This protein family consists almost entirely of two lumazine-binding domains, described in the family Lum_binding from Pfam. The model generates lower scores against other proteins that also have two lumazine-binding domains, including some involved in bioluminescence.The name ribE was selected, from among alternatives including ribB and ribC, to match the usage in EcoCyc. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
Pssm-ID: 272950 Cd Length: 200 Bit Score: 191.86 E-value: 5.29e-62
Lumazine binding domain; This domain binds to derivatives of lumazine in some proteins. Some ...
100-182
7.28e-31
Lumazine binding domain; This domain binds to derivatives of lumazine in some proteins. Some proteins have lost the residues involved in binding lumazine.
Pssm-ID: 459900 Cd Length: 83 Bit Score: 108.26 E-value: 7.28e-31
Riboflavin synthase alpha chain [Coenzyme transport and metabolism]; Riboflavin synthase alpha ...
1-196
3.17e-99
Riboflavin synthase alpha chain [Coenzyme transport and metabolism]; Riboflavin synthase alpha chain is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis
Pssm-ID: 440076 Cd Length: 198 Bit Score: 285.78 E-value: 3.17e-99
Riboflavin synthase and similar proteins; Riboflavin synthase catalyzes the dismutation of two ...
1-185
1.57e-92
Riboflavin synthase and similar proteins; Riboflavin synthase catalyzes the dismutation of two molecules of 6,7-dimethyl-8-(1'-D-ribityl)-lumazine (DMRL) to yield riboflavin (vitamin B12) and 4-ribitylamino-5-amino-2,6-dihydroxypyrimidine (RAADP). Riboflavin synthase is a homotrimer and the catalysis does not require any cofactors. Active sites are located between pairs of monomers, but only one active site catalyzes a reaction, the other two sites are inactive. Humans do not produce riboflavin synthase, and thus it is a good target for antimicrobial agents. This family also include lumazine protein (LumP) from bioluminescent bacteria. LumP serves as an optical transponder in bioluminescence emission.
Pssm-ID: 293928 Cd Length: 185 Bit Score: 268.49 E-value: 1.57e-92
riboflavin synthase, alpha subunit; This protein family consists almost entirely of two ...
1-193
5.29e-62
riboflavin synthase, alpha subunit; This protein family consists almost entirely of two lumazine-binding domains, described in the family Lum_binding from Pfam. The model generates lower scores against other proteins that also have two lumazine-binding domains, including some involved in bioluminescence.The name ribE was selected, from among alternatives including ribB and ribC, to match the usage in EcoCyc. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]
Pssm-ID: 272950 Cd Length: 200 Bit Score: 191.86 E-value: 5.29e-62
Lumazine binding domain; This domain binds to derivatives of lumazine in some proteins. Some ...
100-182
7.28e-31
Lumazine binding domain; This domain binds to derivatives of lumazine in some proteins. Some proteins have lost the residues involved in binding lumazine.
Pssm-ID: 459900 Cd Length: 83 Bit Score: 108.26 E-value: 7.28e-31
Lumazine binding domain; This domain binds to derivatives of lumazine in some proteins. Some ...
3-84
1.20e-29
Lumazine binding domain; This domain binds to derivatives of lumazine in some proteins. Some proteins have lost the residues involved in binding lumazine.
Pssm-ID: 459900 Cd Length: 83 Bit Score: 105.18 E-value: 1.20e-29
lumazine protein; Lumazine protein (LumP) is involved in the bioluminescence of certain marine ...
1-183
9.86e-28
lumazine protein; Lumazine protein (LumP) is involved in the bioluminescence of certain marine bacteria. It serves as an optical transponder in bioluminescence emission. The intense fluorescence of LumP is caused by non-covalently bound 6,7- dimethyl-8-ribityllumazine. Though its amino acid sequence is very similar to riboflavin synthase it functions as a monomer, unlike the riboflavin synthases from eubacteria, yeasts and plants which act as trimers.
Pssm-ID: 293929 Cd Length: 186 Bit Score: 103.65 E-value: 9.86e-28
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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