ID   RIFK_SULTO              Reviewed;         136 AA.
AC   Q971U9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Riboflavin kinase {ECO:0000255|HAMAP-Rule:MF_01285};
DE            Short=RFK {ECO:0000255|HAMAP-Rule:MF_01285};
DE            EC=2.7.1.161 {ECO:0000255|HAMAP-Rule:MF_01285};
DE   AltName: Full=CTP-dependent riboflavin kinase {ECO:0000255|HAMAP-Rule:MF_01285};
DE   AltName: Full=CTP:riboflavin 5'-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01285};
DE   AltName: Full=Flavokinase {ECO:0000255|HAMAP-Rule:MF_01285};
GN   Name=ribK {ECO:0000255|HAMAP-Rule:MF_01285}; OrderedLocusNames=STK_12800;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
CC   -!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of riboflavin
CC       (vitamin B2) to form flavin mononucleotide (FMN). {ECO:0000255|HAMAP-
CC       Rule:MF_01285}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01285};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01285};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01285};
CC   -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC       (CTP route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01285}.
CC   -!- SIMILARITY: Belongs to the archaeal riboflavin kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01285}.
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DR   EMBL; BA000023; BAB66321.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q971U9; -.
DR   SMR; Q971U9; -.
DR   STRING; 273063.STK_12800; -.
DR   EnsemblBacteria; BAB66321; BAB66321; STK_12800.
DR   KEGG; sto:STK_12800; -.
DR   PATRIC; fig|273063.9.peg.1438; -.
DR   eggNOG; arCOG01904; Archaea.
DR   OMA; PYEGTLN; -.
DR   UniPathway; UPA00276; UER00929.
DR   Proteomes; UP000001015; Chromosome.
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; 2.40.30.30; -; 1.
DR   HAMAP; MF_01285; Riboflavin_kinase; 1.
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   PANTHER; PTHR40706; PTHR40706; 1.
DR   Pfam; PF01982; CTP-dep_RFKase; 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..136
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000322080"
FT   BINDING         15..20
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT   BINDING         103
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT   BINDING         111
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT   BINDING         116..119
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
SQ   SEQUENCE   136 AA;  15284 MW;  0FFCB18C7770D092 CRC64;
     MRTKILHIKG KVTAGLGEGR IFLSIPYYIE SFKKYLGFEP YAGTLNIVIY DRISLENRLI
     LDLAKGIIIP EHKEPNRVLG SVKAFPSSIN SISPAAIVIP ARTTHPKSVI EIISPYYLRE
     KLSLKDGDEV EIEVYL