Q84MD8 · FHYRK_ARATH
- ProteinBifunctional riboflavin kinase/FMN phosphatase
- GeneFHY
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids379 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Bifunctional enzyme that catalyzes the hydrolysis of flavin-mononucleotide (FMN) to riboflavin (vitamin B2) and the phosphorylation of riboflavin to form (FMN) coenzyme.
Catalytic activity
- ATP + riboflavin = ADP + FMN + H+
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.03 μM | riboflavin | 7.5 | ||||
2 μM | ATP | 7.5 | ||||
6.74 μM | FMN | 7.5 |
pH Dependence
Optimum pH is acidic (5.5-6.0) for FMN phosphatase activity and basic for riboflavin kinase activity.
Temperature Dependence
Optimum temperature is 55 degrees Celsius.
Pathway
Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 17 | Nucleophile; for FMN phosphatase activity | ||||
Sequence: D | ||||||
Binding site | 17 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 19 | Proton donor; for FMN phosphatase activity | ||||
Sequence: D | ||||||
Binding site | 19 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 248 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 254 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 260 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 260 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 262 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 312 | Nucleophile; for riboflavin kinase activity | ||||
Sequence: E | ||||||
Binding site | 315 | ATP (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 317 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 324 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 337 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 342 | FMN (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | FMN adenylyltransferase activity | |
Molecular Function | FMN hydrolase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | riboflavin kinase activity | |
Biological Process | FMN biosynthetic process | |
Biological Process | riboflavin biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional riboflavin kinase/FMN phosphatase
Including 2 domains:
- Recommended nameFMN phosphatase
- EC number
- Alternative names
- Recommended nameRiboflavin kinase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ84MD8
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000429025 | 2-379 | Bifunctional riboflavin kinase/FMN phosphatase | |||
Sequence: SMSNSLKKLSSCVLIDLDGTLINTDGVVGDILRKYLCKYGKQWDGRESLKIVGKTPVEAATTIVEDYELPCKVDEFNSEFYPLFSAQMDKIKSLPGANRLIRHLKCHGVPVALASNSSRANIESKISYHEGWKECFSVIVGSDEVSKGKPSPDIFLEAAKRLKKDPADCLVIEDSVPGVMAGKAAGTKVIAVPSLPKQTHLYTSADEVINSLLDIRLEKWGLPPFQDWIENTLPIDPWHIGGPVIKGFGRGSKVLGIPTANLSTKDYADELVEHPSGVYFGWAGLAKRGVFKMVMSIGWNPYFNNKEKTIEPWLLHDFTEDFYGEELRLIIVGYIRPEANFSSLESLIAKIHEDREVAEKALDLPSYAKFKGDPYLTK |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Sequence similarities
In the N-terminal section; belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.
In the C-terminal section; belongs to the flavokinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length379
- Mass (Da)42,110
- Last updated2003-06-01 v1
- Checksum01C279F602C86E3F
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY878327 EMBL· GenBank· DDBJ | AAX98488.1 EMBL· GenBank· DDBJ | mRNA | ||
AL022603 EMBL· GenBank· DDBJ | CAA18711.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161555 EMBL· GenBank· DDBJ | CAB81254.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE84457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT006373 EMBL· GenBank· DDBJ | AAP21181.1 EMBL· GenBank· DDBJ | mRNA | ||
AK227237 EMBL· GenBank· DDBJ | BAE99274.1 EMBL· GenBank· DDBJ | mRNA |