RIFK_METB6
ID RIFK_METB6 Reviewed; 222 AA.
AC A7I4M1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Riboflavin kinase;
DE Short=RFK;
DE EC=2.7.1.161;
DE AltName: Full=CTP-dependent riboflavin kinase;
DE AltName: Full=CTP:riboflavin 5'-phosphotransferase;
DE AltName: Full=Flavokinase;
GN Name=ribK; OrderedLocusNames=Mboo_0159;
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
CC -!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of riboflavin
CC (vitamin B2) to form flavin mononucleotide (FMN). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (CTP route): step 1/1.
CC -!- SIMILARITY: Belongs to the archaeal riboflavin kinase family.
CC {ECO:0000305}.
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DR EMBL; CP000780; ABS54682.1; -; Genomic_DNA.
DR RefSeq; WP_011991170.1; NC_009712.1.
DR AlphaFoldDB; A7I4M1; -.
DR SMR; A7I4M1; -.
DR STRING; 456442.Mboo_0159; -.
DR EnsemblBacteria; ABS54682; ABS54682; Mboo_0159.
DR GeneID; 5411539; -.
DR KEGG; mbn:Mboo_0159; -.
DR eggNOG; arCOG01904; Archaea.
DR HOGENOM; CLU_088476_0_0_2; -.
DR OMA; AYYVRQY; -.
DR OrthoDB; 91297at2157; -.
DR UniPathway; UPA00276; UER00929.
DR Proteomes; UP000002408; 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; 1.10.10.10; -; 1.
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 InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR40706; PTHR40706; 1.
DR Pfam; PF01982; CTP-dep_RFKase; 1.
DR SUPFAM; SSF46785; SSF46785; 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..222
FT /note="Riboflavin kinase"
FT /id="PRO_0000322088"
FT REGION 1..92
FT /note="H-T-H motif-like"
FT REGION 93..222
FT /note="Riboflavin kinase"
FT BINDING 102..107
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 201..204
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000250"
SQ SEQUENCE 222 AA; 24729 MW; C079E255C4C8055F CRC64;
MVLAEDLECL KALALMGGMR EPVFISSQTL GEVLETSPQT ASRRLKALEG QRLISRTLNP
DGQHITVTKE GEDGLRREYA EYCRLFAHEG GHYTLPGIVI SGLGEGRYYM SLEPYKKQFL
RHLGFEPYPG TLNLRLSGSD IPTRKKIDSL TWIPIHGFSA EGRTFGEVRC MPCRINDIPC
GIVVPGRSHY PEDIVEVIAP VGLRDALGVK ENDRVNVEVA YD
