ID RIFK_THEAC Reviewed; 220 AA. AC Q9HJA6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 123. 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; OrderedLocusNames=Ta1064; OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC OS 15155 / AMRC-C165). OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales; OC Thermoplasmataceae; Thermoplasma. OX NCBI_TaxID=273075; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165; RX PubMed=11029001; DOI=10.1038/35035069; RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.; RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma RT acidophilum."; RL Nature 407:508-513(2000). CC -!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of riboflavin CC (vitamin B2) to form flavin mononucleotide (FMN). {ECO:0000250}. 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; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin CC (CTP route): step 1/1. CC -!- SIMILARITY: Belongs to the archaeal riboflavin kinase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL445066; CAC12192.1; -; Genomic_DNA. DR RefSeq; WP_010901475.1; NC_002578.1. DR PDB; 3CTA; X-ray; 2.20 A; A=2-220. DR PDB; 5TRD; X-ray; 1.85 A; A/B=2-220. DR PDBsum; 3CTA; -. DR PDBsum; 5TRD; -. DR AlphaFoldDB; Q9HJA6; -. DR SMR; Q9HJA6; -. DR STRING; 273075.gene:9572285; -. DR PaxDb; 273075-Ta1064; -. DR EnsemblBacteria; CAC12192; CAC12192; CAC12192. DR GeneID; 1456578; -. DR KEGG; tac:Ta1064; -. DR eggNOG; arCOG01904; Archaea. DR HOGENOM; CLU_088476_0_0_2; -. DR InParanoid; Q9HJA6; -. DR OrthoDB; 30955at2157; -. DR BRENDA; 2.7.1.161; 6324. DR UniPathway; UPA00276; UER00929. DR EvolutionaryTrace; Q9HJA6; -. DR Proteomes; UP000001024; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0008531; F:riboflavin kinase activity; IEA:InterPro. DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro. DR Gene3D; 2.40.30.30; Riboflavin kinase-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR012318; HTH_CRP. DR InterPro; IPR039063; RibK_CTP-dep. DR InterPro; IPR023602; Riboflavin_kinase_CTP-dep. DR InterPro; IPR023465; Riboflavin_kinase_dom_sf. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR40706; RIBOFLAVIN KINASE; 1. DR PANTHER; PTHR40706:SF1; RIBOFLAVIN KINASE; 1. DR Pfam; PF01982; CTP-dep_RFKase; 1. DR Pfam; PF13545; HTH_Crp_2; 1. DR SUPFAM; SSF82114; Riboflavin kinase-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Flavoprotein; FMN; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..220 FT /note="Riboflavin kinase" FT /id="PRO_0000322106" FT REGION 1..92 FT /note="H-T-H motif-like" FT REGION 93..220 FT /note="Riboflavin kinase" FT BINDING 102..107 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250" FT BINDING 131 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 133 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 188 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 195 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000250" FT BINDING 200..203 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250" FT HELIX 6..18 FT /evidence="ECO:0007829|PDB:5TRD" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:5TRD" FT STRAND 22..26 FT /evidence="ECO:0007829|PDB:5TRD" FT HELIX 28..35 FT /evidence="ECO:0007829|PDB:5TRD" FT HELIX 39..51 FT /evidence="ECO:0007829|PDB:5TRD" FT STRAND 54..60 FT /evidence="ECO:0007829|PDB:5TRD" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:5TRD" FT HELIX 70..86 FT /evidence="ECO:0007829|PDB:5TRD" FT STRAND 93..100 FT /evidence="ECO:0007829|PDB:5TRD" FT HELIX 106..110 FT /evidence="ECO:0007829|PDB:5TRD" FT HELIX 113..123 FT /evidence="ECO:0007829|PDB:5TRD" FT STRAND 132..136 FT /evidence="ECO:0007829|PDB:5TRD" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:5TRD" FT HELIX 141..149 FT /evidence="ECO:0007829|PDB:5TRD" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:5TRD" FT STRAND 168..175 FT /evidence="ECO:0007829|PDB:5TRD" FT STRAND 178..187 FT /evidence="ECO:0007829|PDB:5TRD" FT STRAND 192..197 FT /evidence="ECO:0007829|PDB:5TRD" FT HELIX 202..205 FT /evidence="ECO:0007829|PDB:5TRD" FT STRAND 213..218 FT /evidence="ECO:0007829|PDB:5TRD" SQ SEQUENCE 220 AA; 24997 MW; BB0F694447629612 CRC64; METDDQYYRA IKKIKEAAEA SNRAYLTSSK LADMLGISQQ SASRIIIDLE KNGYITRTVT KRGQILNITE KGLDVLYTEF ADLSRILAIK NNVVITGTVT SGMGEGRYYV ARKQYIIQFQ EKLGIIPYLG TLNIKVDQAS LPELRKIRGF RGIHIEGFKT EDRTFGSVKA FPAKIQNIPC FVIMPERTVY TDVIEIISDK YLREEINLHD GDRVSVEVYT //