AC MF_01285; DC Protein; auto TR HAMAP; MF_01285; -; 1; level=0 XX Names: Riboflavin_kinase XX ID RIFK DE RecName: Full=Riboflavin kinase; DE Short=RFK; DE EC=2.7.1.161; DE AltName: Full=CTP-dependent riboflavin kinase; DE AltName: Full=CTP:riboflavin 5'-phosphotransferase; DE AltName: Full=Flavokinase; GN Name=ribK; XX CC -!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of riboflavin CC (vitamin B2) to form flavin mononucleotide (FMN). CC -!- CATALYTIC ACTIVITY: CC Reaction=CTP + riboflavin = CDP + FMN + H(+); Xref=Rhea:RHEA:25021, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37563, ChEBI:CHEBI:57986, CC ChEBI:CHEBI:58069, ChEBI:CHEBI:58210; EC=2.7.1.161; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin CC (CTP route): step 1/1. CC -!- SIMILARITY: Belongs to the archaeal riboflavin kinase family. XX DR Pfam; PF01982; CTP-dep_RFKase; 1; trigger=no XX KW Flavoprotein KW FMN KW Kinase KW Magnesium KW Metal-binding KW Transferase KW Nucleotide-binding XX GO GO:0000166; F:nucleotide binding GO GO:0000287; F:magnesium ion binding GO GO:0016301; F:kinase activity GO GO:0016773; F:phosphotransferase activity, alcohol group as acceptor GO GO:0009398; P:FMN biosynthetic process XX FT From: RIFK_METJA (Q60365) FT BINDING 10..15 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT BINDING 108..111 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT BINDING 39 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: T FT BINDING 41 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: N FT BINDING 95 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: [TS] FT BINDING 96 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Optional; Condition: Y FT BINDING 103 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: E XX Size: 122-159; Related: None; Template: Q60365; Scope: Archaea Fusion: Nter: Cter: None Duplicate: None Plasmid: 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. XX # Revision 1.20 2022/11/19 //