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UniProt functional annotation for O66529 | ||
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| UniProt code: O66529. |
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| Organism: | |
Aquifex aeolicus (strain VF5). |
| Taxonomy: | |
Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex. |
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| Function: | |
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:11237620, ECO:0000269|PubMed:12603336}. |
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| Catalytic activity: | |
Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D- ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evidence={ECO:0000269|PubMed:11237620, ECO:0000269|PubMed:12603336}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=10.0 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:12603336}; KM=26 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:12603336}; Vmax=31 nmol/min/mg enzyme (at 37 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:12603336}; Vmax=425 nmol/min/mg enzyme (at 70 degrees Celsius and pH 7.0) {ECO:0000269|PubMed:12603336}; Temperature dependence: Extremely thermostable. Has a melting temperature of 119.9 degrees Celsius. {ECO:0000269|PubMed:11237620}; |
| Pathway: | |
Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D- ribitylamino)uracil: step 1/2. {ECO:0000269|PubMed:12684006}. |
| Subunit: | |
Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers. {ECO:0000269|PubMed:11237620}. |
| Similarity: | |
Belongs to the DMRL synthase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.