Q2YN92 · RISA_BRUA2
- ProteinRiboflavin synthase
- GeneribE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids202 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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
Activity regulation
Is inhibited by riboflavin. Product inhibition may be the major mechanism by which RS regulates its enzymatic activity in vivo.
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 binding | |
Molecular Function | riboflavin synthase activity | |
Biological Process | protein homotrimerization | |
Biological Process | riboflavin biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRiboflavin synthase
- EC number
- Short namesRS
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Brucellaceae > Brucella/Ochrobactrum group > Brucella
Accessions
- Primary accessionQ2YN92
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435442 | 1-202 | Riboflavin synthase | |||
Sequence: MFTGIITDIGKVDRVKPLNEGVLLRIETAYDPETIELGASIACSGVCLTVVALPEKGSNARWFEVEAWEEALRLTTISSWQSGRKINLERSLKLGDEMGGHLVFGHVDGQAEIVERKDEGDAVRFTLRAPEELAPFIAQKGSVALDGTSLTVNGVNANEFDVLLIRHSLEVTTWGERKAGDKVNIEIDQLARYAARLAQYQK |
Interaction
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 1-101 | Lumazine-binding 1 | ||||
Sequence: MFTGIITDIGKVDRVKPLNEGVLLRIETAYDPETIELGASIACSGVCLTVVALPEKGSNARWFEVEAWEEALRLTTISSWQSGRKINLERSLKLGDEMGGH | ||||||
Repeat | 102-198 | Lumazine-binding 2 | ||||
Sequence: LVFGHVDGQAEIVERKDEGDAVRFTLRAPEELAPFIAQKGSVALDGTSLTVNGVNANEFDVLLIRHSLEVTTWGERKAGDKVNIEIDQLARYAARLA |
Domain
Each monomer can bind two substrate molecules, yet there is only one active site for the whole trimeric enzyme, which is located at the interface between two neighboring chains and formed by the N-terminal barrel from chain A and the C-terminal barrel from chain B.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length202
- Mass (Da)22,223
- Last updated2006-02-07 v1
- Checksum6265FA459B3C0195
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AM040264 EMBL· GenBank· DDBJ | CAJ10746.1 EMBL· GenBank· DDBJ | Genomic DNA |