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RIFK_METMP
ID   RIFK_METMP              Reviewed;         127 AA.
AC   Q6M0T4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=MMP0184;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF29740.1; -; Genomic_DNA.
DR   RefSeq; WP_011170128.1; NC_005791.1.
DR   AlphaFoldDB; Q6M0T4; -.
DR   SMR; Q6M0T4; -.
DR   STRING; 267377.MMP0184; -.
DR   EnsemblBacteria; CAF29740; CAF29740; MMP0184.
DR   GeneID; 2761170; -.
DR   KEGG; mmp:MMP0184; -.
DR   PATRIC; fig|267377.15.peg.188; -.
DR   eggNOG; arCOG01904; Archaea.
DR   HOGENOM; CLU_140165_0_0_2; -.
DR   OMA; PYEGTLN; -.
DR   OrthoDB; 91297at2157; -.
DR   BioCyc; MMAR267377:MMP_RS01025-MON; -.
DR   UniPathway; UPA00276; UER00929.
DR   Proteomes; UP000000590; 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..127
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000322071"
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;  14345 MW;  0CACEEADA69E0E43 CRC64;
     MEIFGHVVSG LGEGKFFVGL THYKNKFEEL TGFTPFEGTL NVKLKHNFNL DEFNPIEFDG
     FEIDGKKYFG GKVLLIKLFN KQGNSINCAV VAPKKTDHSK KTLEIIAPIQ LRKFLLLKNS
     DVVKLVI
 
 
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