HAMAP rule MF_00178
General rule information
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Accession | MF_00178 |
Dates | 1-JUN-2001 (Created) 1-JUN-2023 (Last updated, Version 37) |
Name | Lumazine_synth |
Scope | Bacteria
Archaea |
Templates | P61714 (RISB_ECOLI); O66529 (RISB_AQUAE); P11998 (RISB_BACSU); P61711 (RISB2_BRUAB); P9WHE9 (RISB_MYCTU); Q81MB5 (RISB_BACAN); Q57DY1 (RISB1_BRUAB); Q986N2 (RISB2_RHILO); Q983B0 (RISB1_RHILO); Q8YGH2 (RISB1_BRUME); Q57751 (RISB_METJA); P66038 (RISB_SALTY); Q2YKV1 (RISB2_BRUA2); Q2YNC6 (RISB1_BRUA2): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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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. |
Catalytic activity | RHEA:26152: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
EC 2.5.1.78 |
Pathway | Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. |
case <OC:Aquificae> or <OC:Bacillales> or <OC:Gammaproteobacteria> or <OC:Methanococci>
Subunit | Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers. |
else case <OC:Mycobacterium>
Subunit | Homopentamer. |
end case
Similarity | Belongs to the DMRL synthase family. |
Keywords
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Gene Ontology
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GO:0000906; Molecular function: 6,7-dimethyl-8-ribityllumazine synthase activity.
GO:0009231; Biological process: riboflavin biosynthetic process.
GO:0009231; Biological process: riboflavin biosynthetic process.
Cross-references
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Features
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From: RISB_AQUAE (O66529) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 56 | 58 | /ligand="5-amino-6-(D-ribitylamino)uracil" /ligand_id="ChEBI:CHEBI:15934 | |||||||||
BINDING | 80 | 82 | /ligand="5-amino-6-(D-ribitylamino)uracil" /ligand_id="ChEBI:CHEBI:15934 | |||||||||
BINDING (Optional) | 85 | 86 | /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate" /ligand_id="ChEBI:CHEBI:58830 | [AQSGEDKTN]-[TS] | ||||||||
ACT_SITE | 88 | 88 | Proton donor | [HR] | ||||||||
BINDING | 22 | 22 | /ligand="5-amino-6-(D-ribitylamino)uracil" /ligand_id="ChEBI:CHEBI:15934 | [FWY] | ||||||||
BINDING | 113 | 113 | /ligand="5-amino-6-(D-ribitylamino)uracil" /ligand_id="ChEBI:CHEBI:15934 | [FNLSDMYIHV] | ||||||||
BINDING | 127 | 127 | /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate" /ligand_id="ChEBI:CHEBI:58830 | [RH] |
Additional information
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Size range | 133-190 amino acids |
Related rules | None |
Fusion | None |
Comments | Lumazine synthase structures are either observed as pentamers, dimers of pentamers or dodecamers of pentamers. |