A0A924I295 · A0A924I295_9SPHN
- Protein6,7-dimethyl-8-ribityllumazine synthase
- GeneribH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids387 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
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
- (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O + H+
Cofactor
Protein has several cofactor binding sites:
Pathway
Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 259 | 5-amino-6-(D-ribitylamino)uracil (UniProtKB | ChEBI) | |||
Binding site | 290-292 | 5-amino-6-(D-ribitylamino)uracil (UniProtKB | ChEBI) | |||
Binding site | 314-316 | 5-amino-6-(D-ribitylamino)uracil (UniProtKB | ChEBI) | |||
Binding site | 319-320 | (2S)-2-hydroxy-3-oxobutyl phosphate (UniProtKB | ChEBI) | |||
Active site | 322 | Proton donor | |||
Binding site | 346 | 5-amino-6-(D-ribitylamino)uracil (UniProtKB | ChEBI) | |||
Binding site | 360 | (2S)-2-hydroxy-3-oxobutyl phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | riboflavin synthase complex | |
Molecular Function | 3,4-dihydroxy-2-butanone-4-phosphate synthase activity | |
Molecular Function | 6,7-dimethyl-8-ribityllumazine synthase activity | |
Molecular Function | GTP cyclohydrolase II activity | |
Molecular Function | metal ion binding | |
Biological Process | riboflavin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name6,7-dimethyl-8-ribityllumazine synthase
- EC number
- Short namesDMRL synthase ; LS ; Lumazine synthase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingosinicellaceae > Sandarakinorhabdus
Accessions
- Primary accessionA0A924I295
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 81-230 | GTP cyclohydrolase II | |||
Sequence similarities
Belongs to the DMRL synthase family.
In the C-terminal section; belongs to the GTP cyclohydrolase II family.
In the N-terminal section; belongs to the DHBP synthase family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length387
- Mass (Da)41,025
- Last updated2023-02-22 v1
- ChecksumF1771AE9720D0704
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 1 | ||||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JACMPU010000032 EMBL· GenBank· DDBJ | MBC7519610.1 EMBL· GenBank· DDBJ | Genomic DNA |