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RIFK_METM6
ID   RIFK_METM6              Reviewed;         127 AA.
AC   A9A8B2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=MmarC6_0768;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-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; CP000867; ABX01585.1; -; Genomic_DNA.
DR   RefSeq; WP_012193477.1; NC_009975.1.
DR   AlphaFoldDB; A9A8B2; -.
DR   SMR; A9A8B2; -.
DR   STRING; 444158.MmarC6_0768; -.
DR   EnsemblBacteria; ABX01585; ABX01585; MmarC6_0768.
DR   GeneID; 5737881; -.
DR   KEGG; mmx:MmarC6_0768; -.
DR   eggNOG; arCOG01904; Archaea.
DR   HOGENOM; CLU_140165_0_0_2; -.
DR   OMA; PYEGTLN; -.
DR   OrthoDB; 91297at2157; -.
DR   PhylomeDB; A9A8B2; -.
DR   UniPathway; UPA00276; UER00929.
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_1000140370"
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;  14320 MW;  D373005A0ACDF839 CRC64;
     MEIFGNVVSG LGEGSFFVGL TPYKYKFKEL TGFTPFEGTL NVKLKHNFNL DEFNPIEFDG
     FEIDGKKYFG GKVLLIKLFN KSGHSIDCAI VAPKKTDHSK KTLEIIAPIQ LRKFLSLKNF
     DVVKIVI
 
 
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