ID   RIFK_METS5              Reviewed;         217 AA.
AC   A4YHJ0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Msed_1737;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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}.
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DR   EMBL; CP000682; ABP95892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4YHJ0; -.
DR   SMR; A4YHJ0; -.
DR   STRING; 399549.Msed_1737; -.
DR   EnsemblBacteria; ABP95892; ABP95892; Msed_1737.
DR   KEGG; mse:Msed_1737; -.
DR   eggNOG; arCOG01904; Archaea.
DR   HOGENOM; CLU_088476_0_0_2; -.
DR   OMA; AYYVRQY; -.
DR   UniPathway; UPA00276; UER00929.
DR   Proteomes; UP000000242; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008531; F:riboflavin kinase activity; IEA:InterPro.
DR   GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 2.40.30.30; -; 1.
DR   HAMAP; MF_01285; Riboflavin_kinase; 1.
DR   InterPro; IPR000835; HTH_MarR-typ.
DR   InterPro; IPR039063; RibK_CTP-dep.
DR   InterPro; IPR023470; Riboflavin_kinase_archaeal.
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; PTHR40706; 1.
DR   Pfam; PF01982; CTP-dep_RFKase; 1.
DR   Pfam; PF12802; MarR_2; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF82114; SSF82114; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..217
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000322095"
FT   REGION          1..86
FT                   /note="H-T-H motif-like"
FT   REGION          87..217
FT                   /note="Riboflavin kinase"
FT   BINDING         96..101
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         197..200
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  24661 MW;  C913F01E1E294DEB CRC64;
     MSDECLIAKI VYLSLQQKEV TQQMIADELK MSQQSVSRKL KELEERNLVR RSLSKEGEII
     RVTENGEKLL EDCLSMMRAT IISSHVLEIR GRATSGLGEG RIFLSMPYYM ESFKKFLGFE
     PYPGTLNLVI YDRISLENRL VLDISKAINI PEHKEENRVL GAVRAFPASV NDLKPAAVVF
     PLRSVHPKSV IEVISPYHLR KELNIKDGDE VVIQAYA