A0A0H3APR9 · A0A0H3APR9_BRUO2
- ProteinRiboflavin synthase
- GeneribE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids202 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
Function
function
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.
Catalytic activity
- 2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H+ = 5-amino-6-(D-ribitylamino)uracil + riboflavin
Pathway
Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 4-6 | 2,4-dihydroxypteridine 1 (UniProtKB | ChEBI) | ||||
Sequence: GII | ||||||
Binding site | 47-49 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners | ||||
Sequence: CLT | ||||||
Binding site | 66-68 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners | ||||
Sequence: EAW | ||||||
Binding site | 105-107 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners | ||||
Sequence: GHV | ||||||
Binding site | 140 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 149-151 | 2,4-dihydroxypteridine 1 (UniProtKB | ChEBI) | ||||
Sequence: SLT | ||||||
Binding site | 163-168 | 2,4-dihydroxypteridine 1 (UniProtKB | ChEBI) | ||||
Sequence: LLIRHS |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | riboflavin synthase activity | |
Biological Process | riboflavin biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRiboflavin synthase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Brucellaceae > Brucella/Ochrobactrum group > Brucella
Accessions
- Primary accessionA0A0H3APR9
Proteomes
Structure
Family & Domains
Features
Showing features for domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-101 | Lumazine-binding | ||||
Sequence: MFTGIITDIGKVDRVKPLNEGVLLRIETAYDPETIELGASIACSGVCLTVVALPEKGSNARWFEVEAWEEALRLTTISNWQSGRKINLERSLKLGDEMGGH | ||||||
Repeat | 1-101 | Lumazine-binding | ||||
Sequence: MFTGIITDIGKVDRVKPLNEGVLLRIETAYDPETIELGASIACSGVCLTVVALPEKGSNARWFEVEAWEEALRLTTISNWQSGRKINLERSLKLGDEMGGH | ||||||
Domain | 102-198 | Lumazine-binding | ||||
Sequence: LVSGHVDGQAEIVERKDEGDAVRFTLRAPEELAPFIAQKGSVALDGTSLTVNGVNANEFDVLLIRHSLEVTTWGECKAGDKVNIEIDQLARYAARLA | ||||||
Repeat | 102-198 | Lumazine-binding | ||||
Sequence: LVSGHVDGQAEIVERKDEGDAVRFTLRAPEELAPFIAQKGSVALDGTSLTVNGVNANEFDVLLIRHSLEVTTWGECKAGDKVNIEIDQLARYAARLA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length202
- Mass (Da)22,137
- Last updated2015-09-16 v1
- Checksum837506E30697DAF8
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000708 EMBL· GenBank· DDBJ | ABQ60518.1 EMBL· GenBank· DDBJ | Genomic DNA |