2.5.1.9: riboflavin synthase
This is an abbreviated version!
For detailed information about riboflavin synthase, go to the full flat file.
Word Map on EC 2.5.1.9
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2.5.1.9
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6,7-dimethyl-8-ribityllumazine
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cyclohydrolase
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5-amino-6-ribitylamino-2,41h,3h-pyrimidinedione
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dismutation
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guilliermondii
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3,4-dihydroxy-2-butanone
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icosahedral
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bartonellae
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photobacterium
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flavinogenic
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flavinogenesis
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ashbyii
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eremothecium
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ribitylated
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leiognathi
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henselae
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famata
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drug development
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pharmacology
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medicine
- 2.5.1.9
- 6,7-dimethyl-8-ribityllumazine
-
cyclohydrolase
-
5-amino-6-ribitylamino-2,41h,3h-pyrimidinedione
-
dismutation
- guilliermondii
- 3,4-dihydroxy-2-butanone
-
icosahedral
-
bartonellae
- photobacterium
-
flavinogenic
-
flavinogenesis
-
ashbyii
- eremothecium
-
ribitylated
- leiognathi
- henselae
- famata
- drug development
- pharmacology
- medicine
Reaction
2 6,7-dimethyl-8-(1-D-ribityl)lumazine = +
Synonyms
heavy riboflavin synthase, light riboflavin synthase, lumazine synthase/riboflavin synthase complex, RibD, RibE1, riboflavin synthase, riboflavin synthetase, riboflavine synthase, riboflavine synthetase, synthase, riboflavin
ECTree
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Subunits
Subunits on EC 2.5.1.9 - riboflavin synthase
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homotrimer
pentamer
polymer
trimer
additional information
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each subunit comprising two beta-barrel catalytic domains (residues 1-179), a coiled-coil segment (residues 180-195), and a structurally disordered C-terminal extension (residues 196-207)
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60 * 16000-16200 (beta) + 3 * 23500 (alpha), heavy riboflavin synthase, X-ray studies, analytical ultracentrifugation
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2 folding topologies, the active site can be formed at the subunit interface or each subunit binds one substrate molecule
trimer
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3 * 21171, recombinant enzyme expressed from synthetic gene, electrospray mass spectrometry
trimer
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folding topology, the active site can be formed at the subunit interface
trimer
subunit fold and arrangement, beta-barrel capped by short alpha-helices on each side, overview
trimer
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folding topology, each subunit binds one substrate molecule
each subunit of the homotrimer consists of 2 domains
additional information
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each subunit of the homotrimer consists of 2 domains
additional information
structure model, biological implication
additional information
2 similar folding domains per subunit
additional information
N-terminal sequence is MFTGIVEELGEITAV