P57212 · RISA_BUCAI
- ProteinRiboflavin synthase
- GeneribE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids208 (go to sequence)
- Protein existenceInferred from homology
- 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 | 48-50 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners | ||||
Sequence: CLT | ||||||
Binding site | 62-67 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners | ||||
Sequence: DVIQET | ||||||
Binding site | 101-103 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners | ||||
Sequence: GHV | ||||||
Binding site | 137 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 146-148 | 2,4-dihydroxypteridine 1 (UniProtKB | ChEBI) | ||||
Sequence: SLT | ||||||
Binding site | 160-165 | 2,4-dihydroxypteridine 1 (UniProtKB | ChEBI) | ||||
Sequence: NIIPYT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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
- Short namesRS
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Buchnera
Accessions
- Primary accessionP57212
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000068160 | 1-208 | Riboflavin synthase | |||
Sequence: MFTGIINGTATIVYIEKKKKKYRYTVELPSNLSKNLKLGDSISHNGCCLTVKLINNSFIICDVIQETLKSTNLGILNIGDSINIERSIKYGDEIGGHIISGHVMNTAEISKMSKSDNNCVIWLKMNNMSLMKYIFYKGFICVDGISLTVNDIIKNEFCVNIIPYTFLFTTIKDKKNGSLVNIEIDFYTQTIVDTTERLINNNLKSLYD |
Interaction
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 1-97 | Lumazine-binding 1 | ||||
Sequence: MFTGIINGTATIVYIEKKKKKYRYTVELPSNLSKNLKLGDSISHNGCCLTVKLINNSFIICDVIQETLKSTNLGILNIGDSINIERSIKYGDEIGGH | ||||||
Repeat | 98-195 | Lumazine-binding 2 | ||||
Sequence: IISGHVMNTAEISKMSKSDNNCVIWLKMNNMSLMKYIFYKGFICVDGISLTVNDIIKNEFCVNIIPYTFLFTTIKDKKNGSLVNIEIDFYTQTIVDTT |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length208
- Mass (Da)23,505
- Last updated2000-12-01 v1
- Checksum7CCE3272CF54BA5B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000003 EMBL· GenBank· DDBJ | BAB12830.1 EMBL· GenBank· DDBJ | Genomic DNA |