RIFK_HALWD
ID RIFK_HALWD Reviewed; 234 AA.
AC Q18FC4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=HQ_3236A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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; AM180088; CAJ53334.1; -; Genomic_DNA.
DR RefSeq; WP_011572439.1; NC_008212.1.
DR AlphaFoldDB; Q18FC4; -.
DR SMR; Q18FC4; -.
DR STRING; 362976.HQ_3236A; -.
DR EnsemblBacteria; CAJ53334; CAJ53334; HQ_3236A.
DR GeneID; 4193356; -.
DR KEGG; hwa:HQ_3236A; -.
DR eggNOG; arCOG01904; Archaea.
DR HOGENOM; CLU_088476_0_0_2; -.
DR OMA; AYYVRQY; -.
DR UniPathway; UPA00276; UER00929.
DR Proteomes; UP000001975; 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 CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.40.30.30; -; 1.
DR HAMAP; MF_01285; Riboflavin_kinase; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
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..234
FT /note="Riboflavin kinase"
FT /id="PRO_0000322086"
FT REGION 1..98
FT /note="H-T-H motif-like"
FT REGION 99..234
FT /note="Riboflavin kinase"
FT BINDING 108..113
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 212..215
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000250"
SQ SEQUENCE 234 AA; 25870 MW; 42FF0A066A196558 CRC64;
MAESTTAVGH DELAALKFVA LEGAHSEPIK ISCSELSDRL DASSQTASRR LQRLEAAGYL
DRDVVTDGQW VSLTKAGETA LHKEYTQYQE IFGDNSSVVE LTGTVTSGMG EGRHYISLSG
YMKQFRERLG YEPFPGTLNI DLDDDSTRTR VAVSSLTGIQ IDGWEDDERT FGPATCYPAE
IILAEQTAEA AHIIVPERTH HDETQLEVIA PERLRDSLEL TDGQRITVQL KPKE
