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HAMAP rule MF_01285

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General rule information [?]

Accession MF_01285
Dates 5-FEB-2008 (Created)
19-NOV-2022 (Last updated, Version 20)
Name Riboflavin_kinase
Template Q60365 (RIFK_METJA)

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Riboflavin kinase;
AltName: Full=CTP-dependent riboflavin kinase;
AltName: Full=CTP:riboflavin 5'-phosphotransferase;
AltName: Full=Flavokinase;
Gene name

Comments [?]

Function Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
Catalytic activity RHEA:25021: CTP + riboflavin = CDP + FMN + H(+)
Cofactor Mg(2+)
Note: Binds 1 Mg(2+) ion per subunit.
Pathway Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
Similarity Belongs to the archaeal riboflavin kinase family.

Keywords [?]

Gene Ontology [?]

GO:0000166; Molecular function: nucleotide binding.
GO:0000287; Molecular function: magnesium ion binding.
GO:0016301; Molecular function: kinase activity.
GO:0016773; Molecular function: phosphotransferase activity, alcohol group as acceptor.
GO:0009398; Biological process: FMN biosynthetic process.

Cross-references [?]

Pfam PF01982; CTP-dep_RFKase; 1;

Features [?]

From: RIFK_METJA (Q60365)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     10     15       /ligand="CDP" /ligand_id="ChEBI:CHEBI:58069        
BINDING     108     111       /ligand="CDP" /ligand_id="ChEBI:CHEBI:58069        
BINDING     39     39       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420     T  
BINDING     41     41       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420     N  
BINDING     95     95       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     [TS]  
BINDING (Optional)     96     96       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     Y  
BINDING     103     103       /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210     E  

Additional information [?]

Size range 122-159 amino acids
Related rules None
Fusion Nter: <Unknown>; Cter: None
Comments Many family members are N-terminally fused with a putative winged HTH DNA-binding domain, that has not been annotated because of bad score and truncation. Possible wrong start in SULAC. Longer N-terminus in SACS2 and IGNH4.