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RIFK_PYRFU
ID   RIFK_PYRFU              Reviewed;         212 AA.
AC   Q8U262;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=PF0988;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81112.1; -; Genomic_DNA.
DR   RefSeq; WP_011012125.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U262; -.
DR   SMR; Q8U262; -.
DR   STRING; 186497.PF0988; -.
DR   PRIDE; Q8U262; -.
DR   EnsemblBacteria; AAL81112; AAL81112; PF0988.
DR   GeneID; 41712801; -.
DR   KEGG; pfu:PF0988; -.
DR   PATRIC; fig|186497.12.peg.1047; -.
DR   eggNOG; arCOG01904; Archaea.
DR   HOGENOM; CLU_088476_0_0_2; -.
DR   OMA; AYYVRQY; -.
DR   OrthoDB; 91297at2157; -.
DR   PhylomeDB; Q8U262; -.
DR   UniPathway; UPA00276; UER00929.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; IPR012318; HTH_CRP.
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; PF13545; HTH_Crp_2; 1.
DR   SMART; SM00347; HTH_MARR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF82114; SSF82114; 1.
DR   PROSITE; PS50995; HTH_MARR_2; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..212
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000322102"
FT   REGION          1..87
FT                   /note="H-T-H motif-like"
FT   REGION          88..212
FT                   /note="Riboflavin kinase"
FT   BINDING         97..102
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         193..196
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  23813 MW;  F2AB341CB6E2070A CRC64;
     MKKSNLDLLI LLAKAGGIEK EILTTSRELS KMLNVSPQTI VRWLEDLEKD GLIKKSESRK
     GTLVTITEEG VKFLEKLHEE LSDALYRGII IGEVVSGIGE GAYYVRQYAP LIREYLGFDP
     YPGTLNVRVI FPKTIFDALC NVRPIIIPGF TKEGRTFGDV RAYRVKIDNI EGAIVIPSRT
     IHPPKIAEII APVNLRKTLN LKDGDRIRIK TL
 
 
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