P45273 · RISA_HAEIN
- ProteinRiboflavin synthase
- GeneribE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids204 (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: GIV | ||||||
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: DLMQET | ||||||
Binding site | 101-103 | 2,4-dihydroxypteridine 2 (UniProtKB | ChEBI); ligand shared between two trimeric partners | ||||
Sequence: GHI | ||||||
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: NLIPET |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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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 > Pasteurellales > Pasteurellaceae > Haemophilus
Accessions
- Primary accessionP45273
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000068167 | 1-204 | Riboflavin synthase | |||
Sequence: MFTGIVQGTAPIHSIKEKANFRTQVVKLLPEMRKDLEIGASIANNGVCLTVTEINGDLVSFDLMQETLKITNLGTVKVGDYVNIERAMQMGTEIGGHLLSGHIYCTAKISDIIASENNRQIWFELPSADVMKYILTKGFVAVDGISLTIGEVRDTQFCVNLIPETLQRTLMGRRKVGDIVNIEIDPQTQAIVDTVENYLQSKNF |
Interaction
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 1-97 | Lumazine-binding 1 | ||||
Sequence: MFTGIVQGTAPIHSIKEKANFRTQVVKLLPEMRKDLEIGASIANNGVCLTVTEINGDLVSFDLMQETLKITNLGTVKVGDYVNIERAMQMGTEIGGH | ||||||
Repeat | 98-195 | Lumazine-binding 2 | ||||
Sequence: LLSGHIYCTAKISDIIASENNRQIWFELPSADVMKYILTKGFVAVDGISLTIGEVRDTQFCVNLIPETLQRTLMGRRKVGDIVNIEIDPQTQAIVDTV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length204
- Mass (Da)22,590
- Last updated1995-11-01 v1
- ChecksumB7C2172F88BC1DA4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L42023 EMBL· GenBank· DDBJ | AAC23257.1 EMBL· GenBank· DDBJ | Genomic DNA |