Q9PJZ1 · RISA_CHLMU
- ProteinRiboflavin synthase
- GeneribE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids198 (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 | 46-48 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners | ||||
Sequence: CLT | ||||||
Binding site | 60-65 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners | ||||
Sequence: DVTEET | ||||||
Binding site | 99-101 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners | ||||
Sequence: GHV | ||||||
Binding site | 130 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 139-141 | 2,4-dihydroxypteridine 1 (UniProtKB | ChEBI) | ||||
Sequence: SLT | ||||||
Binding site | 153-158 | 2,4-dihydroxypteridine 1 (UniProtKB | ChEBI) | ||||
Sequence: SVIPET |
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
- Short namesRS
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Chlamydiota > Chlamydiia > Chlamydiales > Chlamydiaceae > Chlamydia/Chlamydophila group > Chlamydia
Accessions
- Primary accessionQ9PJZ1
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000068163 | 1-198 | Riboflavin synthase | |||
Sequence: MFSGIIQEVARVDLIHHYGDSMEIGIFARNLVDGVPGSSIAVDGICLTLVKREFELLFFDVTEETMACTTIKNYTVGSMVNLERSVRLGDEIGGHFVSGHVCGVGTIIAVEKSYMFFKAPTNLVPYVLEKGFIAIDGISLTIAQVRGDIFSVSVIPETRARTSLGYKQVGSHVNMEPDMMTKMQVDTVMRFQAEKIGK |
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 1-95 | Lumazine-binding 1 | ||||
Sequence: MFSGIIQEVARVDLIHHYGDSMEIGIFARNLVDGVPGSSIAVDGICLTLVKREFELLFFDVTEETMACTTIKNYTVGSMVNLERSVRLGDEIGGH | ||||||
Repeat | 96-188 | Lumazine-binding 2 | ||||
Sequence: FVSGHVCGVGTIIAVEKSYMFFKAPTNLVPYVLEKGFIAIDGISLTIAQVRGDIFSVSVIPETRARTSLGYKQVGSHVNMEPDMMTKMQVDTV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length198
- Mass (Da)21,761
- Last updated2000-10-01 v1
- Checksum8C6218EFBD94C318
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE002160 EMBL· GenBank· DDBJ | AAF39502.1 EMBL· GenBank· DDBJ | Genomic DNA |