RIFK_HYPBU
ID RIFK_HYPBU Reviewed; 149 AA.
AC A2BK57;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=Hbut_0506;
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=17350933; DOI=10.1155/2007/745987;
RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.-P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
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; CP000493; ABM80368.1; -; Genomic_DNA.
DR RefSeq; WP_011821686.1; NC_008818.1.
DR AlphaFoldDB; A2BK57; -.
DR SMR; A2BK57; -.
DR STRING; 415426.Hbut_0506; -.
DR EnsemblBacteria; ABM80368; ABM80368; Hbut_0506.
DR GeneID; 4781463; -.
DR KEGG; hbu:Hbut_0506; -.
DR eggNOG; arCOG01904; Archaea.
DR HOGENOM; CLU_140165_0_0_2; -.
DR OMA; RELASMC; -.
DR OrthoDB; 116081at2157; -.
DR UniPathway; UPA00276; UER00929.
DR Proteomes; UP000002593; 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..149
FT /note="Riboflavin kinase"
FT /id="PRO_0000322066"
FT BINDING 18..23
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 105
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 113
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 118..121
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
SQ SEQUENCE 149 AA; 16712 MW; 5E3054CD6CBE2A94 CRC64;
MENGAVQQLQ LLGKRVKGFG VGGRYVAHPY YSGRFRELLG CTPFPGTLNF DANLDWRELA
SMCEPQVIPG TVWDGVRLGA VYVWKAKIMT RHGYVDCAVI RPLLSGHPPT VLEIVACEKL
EPILENNPDK TVIVTIACKR GDALRWRRY
