ID   RIFK_PYRCJ              Reviewed;         212 AA.
AC   A3MV29;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Pcal_1071;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000561; ABO08496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MV29; -.
DR   SMR; A3MV29; -.
DR   STRING; 410359.Pcal_1071; -.
DR   EnsemblBacteria; ABO08496; ABO08496; Pcal_1071.
DR   KEGG; pcl:Pcal_1071; -.
DR   eggNOG; arCOG01904; Archaea.
DR   HOGENOM; CLU_088476_0_0_2; -.
DR   OMA; AYYVRQY; -.
DR   UniPathway; UPA00276; UER00929.
DR   Proteomes; UP000001431; 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   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR40706; PTHR40706; 1.
DR   Pfam; PF01982; CTP-dep_RFKase; 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   Transferase.
FT   CHAIN           1..212
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000322101"
FT   REGION          1..83
FT                   /note="Unknown"
FT   REGION          84..212
FT                   /note="Riboflavin kinase"
FT   BINDING         93..98
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         179
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         192..195
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  23505 MW;  55FB8E799B8F28F1 CRC64;
     MTELYCERKT LADLIAFASV EGLPVGEAAK RLCMSRQGAY KAVKALREAG YLSEGPVIKL
     TQKGRDALSI VLRNLLRYFD IASIKLVGRV VTGLGEGAFY MSLEGYRRAI ERELGFTPYP
     GTLNIKLEPQ SLAHRRYLDG LPGIHIPGFT NGMRTYGAVK AFRARLADVE GAVVMPERTH
     HPVDVIEFIA PVRVRDVLGL KDGDRVELEV YL