RIFK_METM5
ID RIFK_METM5 Reviewed; 127 AA.
AC A4G005;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
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=MmarC5_1492;
OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=402880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC BAA-1333;
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., Chertkov O., Brettin T., Bruce D., Han C.,
RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL Submitted (MAR-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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABO35789.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000609; ABO35789.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048058521.1; NC_009135.1.
DR AlphaFoldDB; A4G005; -.
DR SMR; A4G005; -.
DR STRING; 402880.MmarC5_1492; -.
DR EnsemblBacteria; ABO35789; ABO35789; MmarC5_1492.
DR GeneID; 4927757; -.
DR KEGG; mmq:MmarC5_1492; -.
DR eggNOG; arCOG01904; Archaea.
DR HOGENOM; CLU_140165_0_0_2; -.
DR OrthoDB; 91297at2157; -.
DR UniPathway; UPA00276; UER00929.
DR Proteomes; UP000000253; 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 Transferase.
FT CHAIN 1..127
FT /note="Riboflavin kinase"
FT /id="PRO_0000322072"
FT BINDING 10..15
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 96
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 104
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 109..112
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
SQ SEQUENCE 127 AA; 14362 MW; 689D65F259C22AFA CRC64;
MEIFGNVVSG LGEGRFFVGL TPYKNKFEEL TGFIPFEGTL NVKLKHNFNL DNFNPIEFDG
FEINGKRYFG GKVLLIKLFN KHGNFVNCAI VAPKKTDHSK KTLEIIAPIQ LRKFLSLNNS
NVVKIVI
