RIFK_PYRAB
ID RIFK_PYRAB Reviewed; 212 AA.
AC Q9UYX4; G8ZHI9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=PYRAB13830; ORFNames=PAB0917;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248287; CAB50288.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70826.1; -; Genomic_DNA.
DR PIR; C75049; C75049.
DR RefSeq; WP_010868498.1; NC_000868.1.
DR AlphaFoldDB; Q9UYX4; -.
DR SMR; Q9UYX4; -.
DR STRING; 272844.PAB0917; -.
DR EnsemblBacteria; CAB50288; CAB50288; PAB0917.
DR GeneID; 1496772; -.
DR KEGG; pab:PAB0917; -.
DR PATRIC; fig|272844.11.peg.1470; -.
DR eggNOG; arCOG01904; Archaea.
DR HOGENOM; CLU_088476_0_0_2; -.
DR OMA; AYYVRQY; -.
DR OrthoDB; 91297at2157; -.
DR PhylomeDB; Q9UYX4; -.
DR UniPathway; UPA00276; UER00929.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 Transferase.
FT CHAIN 1..212
FT /note="Riboflavin kinase"
FT /id="PRO_0000322098"
FT REGION 1..87
FT /note="H-T-H motif-like"
FT REGION 88..212
FT /note="Riboflavin kinase"
FT BINDING 97..102
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 193..196
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000250"
SQ SEQUENCE 212 AA; 23918 MW; 4A420F3ACA03C82A CRC64;
MKMKTLFLLI KLAKMGAIGK EITVTMRELS RELDVSPQTV LRWLEELKEQ GYIHKRESRK
GTLVELTEKG INLLEKLYEE ISTALYSGFI VGEVISGIGE GAYYVRQYAP LIREYLGFDP
YPGTLNVRVL FPKTIFDALC TARPIIIPGF TRNGRTFGDV RAYRVRIDGI EGAIVIPSRT
VHPPKIAEII APVKLRDALN LKDGDKVRIE VV
