RIFK_META3
ID RIFK_META3 Reviewed; 128 AA.
AC A6UVI4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Maeo_0925;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL Submitted (JUN-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}.
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DR EMBL; CP000743; ABR56506.1; -; Genomic_DNA.
DR RefSeq; WP_011973638.1; NC_009635.1.
DR AlphaFoldDB; A6UVI4; -.
DR SMR; A6UVI4; -.
DR STRING; 419665.Maeo_0925; -.
DR EnsemblBacteria; ABR56506; ABR56506; Maeo_0925.
DR GeneID; 5326323; -.
DR KEGG; mae:Maeo_0925; -.
DR eggNOG; arCOG01904; Archaea.
DR HOGENOM; CLU_140165_0_0_2; -.
DR OMA; PYEGTLN; -.
DR OrthoDB; 91297at2157; -.
DR UniPathway; UPA00276; UER00929.
DR Proteomes; UP000001106; 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..128
FT /note="Riboflavin kinase"
FT /id="PRO_0000322070"
FT BINDING 12..17
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
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 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT BINDING 97
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
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 110..113
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
SQ SEQUENCE 128 AA; 14934 MW; 867B600AD6DBBC54 CRC64;
MLNKLFGRVV SGKGEGKHYM SLPPYKEKFK NILGFEPYEG TLNVKLGYII NLNELNPIEV
DDFYYKNNKY YGVKLIPVRI CIKDYCVNGA IVYPKKTEHP NNVIELIAPI KLRKYLSLKN
NYMVKIRL
