ID   RIFK_THEKO              Reviewed;         211 AA.
AC   Q5JGN9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=TK1272;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD85461.1; -; Genomic_DNA.
DR   RefSeq; WP_011250223.1; NC_006624.1.
DR   AlphaFoldDB; Q5JGN9; -.
DR   SMR; Q5JGN9; -.
DR   STRING; 69014.TK1272; -.
DR   EnsemblBacteria; BAD85461; BAD85461; TK1272.
DR   GeneID; 3233889; -.
DR   KEGG; tko:TK1272; -.
DR   PATRIC; fig|69014.16.peg.1244; -.
DR   eggNOG; arCOG01904; Archaea.
DR   HOGENOM; CLU_088476_0_0_2; -.
DR   InParanoid; Q5JGN9; -.
DR   OMA; AYYVRQY; -.
DR   OrthoDB; 91297at2157; -.
DR   PhylomeDB; Q5JGN9; -.
DR   UniPathway; UPA00276; UER00929.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0003677; F:DNA binding; 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:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; IPR012318; HTH_CRP.
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; PF13545; HTH_Crp_2; 1.
DR   SMART; SM00419; HTH_CRP; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF82114; SSF82114; 1.
DR   PROSITE; PS51063; HTH_CRP_2; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..211
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000322105"
FT   REGION          1..85
FT                   /note="H-T-H motif-like"
FT   REGION          86..211
FT                   /note="Riboflavin kinase"
FT   BINDING         95..100
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         191..194
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   211 AA;  23441 MW;  97B9AFA0DD0A78AA CRC64;
     MKKILMLIEL SERNAIGRPV RITIRELADA LNTSPQTVLR LLAELEDEGL IERKTEGRRT
     YIEILPKGLD FLQDICDKIS NALSKGVIVG EVVSGLGEGA YYVRQYEPLI EEYLGFKPFP
     GTLNVKILFP KTVLDAVCNI RPVIIPGFVK DGRTFGDVKA YPVMIGGIKG AIVVPSRTIH
     PPRIAEIIAP VNLREALKLK DGDRVRLEVI Q