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 subunit; This protein family consists almost entirely of two ...
1-200
2.55e-115
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: 326.68 E-value: 2.55e-115
Riboflavin synthase alpha chain [Coenzyme transport and metabolism]; Riboflavin synthase alpha ...
1-200
5.31e-107
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: 305.81 E-value: 5.31e-107
Riboflavin synthase and similar proteins; Riboflavin synthase catalyzes the dismutation of two ...
1-185
2.93e-98
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: 283.12 E-value: 2.93e-98
Lumazine binding domain; This domain binds to derivatives of lumazine in some proteins. Some ...
3-86
4.37e-30
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: 106.33 E-value: 4.37e-30
riboflavin synthase, alpha subunit; This protein family consists almost entirely of two ...
1-200
2.55e-115
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: 326.68 E-value: 2.55e-115
Riboflavin synthase alpha chain [Coenzyme transport and metabolism]; Riboflavin synthase alpha ...
1-200
5.31e-107
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: 305.81 E-value: 5.31e-107
Riboflavin synthase and similar proteins; Riboflavin synthase catalyzes the dismutation of two ...
1-185
2.93e-98
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: 283.12 E-value: 2.93e-98
lumazine protein; Lumazine protein (LumP) is involved in the bioluminescence of certain marine ...
1-186
1.45e-48
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: 157.19 E-value: 1.45e-48
Lumazine binding domain; This domain binds to derivatives of lumazine in some proteins. Some ...
3-86
4.37e-30
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: 106.33 E-value: 4.37e-30
Lumazine binding domain; This domain binds to derivatives of lumazine in some proteins. Some ...
100-184
7.15e-28
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: 100.55 E-value: 7.15e-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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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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