ID F0LK07_THEBM Unreviewed; 211 AA.
AC F0LK07;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Riboflavin kinase {ECO:0000256|ARBA:ARBA00017394, ECO:0000256|HAMAP-Rule:MF_01285};
DE Short=RFK {ECO:0000256|HAMAP-Rule:MF_01285};
DE EC=2.7.1.161 {ECO:0000256|ARBA:ARBA00011987, ECO:0000256|HAMAP-Rule:MF_01285};
DE AltName: Full=CTP-dependent riboflavin kinase {ECO:0000256|ARBA:ARBA00030544, ECO:0000256|HAMAP-Rule:MF_01285};
DE AltName: Full=CTP:riboflavin 5'-phosphotransferase {ECO:0000256|ARBA:ARBA00033116, ECO:0000256|HAMAP-Rule:MF_01285};
DE AltName: Full=Flavokinase {ECO:0000256|ARBA:ARBA00029789, ECO:0000256|HAMAP-Rule:MF_01285};
GN Name=ribK {ECO:0000256|HAMAP-Rule:MF_01285};
GN OrderedLocusNames=TERMP_00567 {ECO:0000313|EMBL:ADT83544.1};
OS Thermococcus barophilus (strain DSM 11836 / MP).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT83544.1, ECO:0000313|Proteomes:UP000007478};
RN [1] {ECO:0000313|EMBL:ADT83544.1, ECO:0000313|Proteomes:UP000007478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX PubMed=21217005; DOI=10.1128/JB.01490-10;
RA Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT "Complete genome sequence of the hyperthermophilic, piezophilic,
RT heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL J. Bacteriol. 193:1481-1482(2011).
CC -!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of riboflavin
CC (vitamin B2) to form flavin mononucleotide (FMN).
CC {ECO:0000256|ARBA:ARBA00003072, ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00000663, ECO:0000256|HAMAP-
CC Rule:MF_01285};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01285};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01285};
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (CTP route): step 1/1. {ECO:0000256|ARBA:ARBA00005219,
CC ECO:0000256|HAMAP-Rule:MF_01285}.
CC -!- SIMILARITY: Belongs to the archaeal riboflavin kinase family.
CC {ECO:0000256|ARBA:ARBA00006428, ECO:0000256|HAMAP-Rule:MF_01285}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01285}.
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DR EMBL; CP002372; ADT83544.1; -; Genomic_DNA.
DR RefSeq; WP_013466842.1; NC_014804.1.
DR AlphaFoldDB; F0LK07; -.
DR GeneID; 10040885; -.
DR KEGG; tba:TERMP_00567; -.
DR PATRIC; fig|391623.17.peg.568; -.
DR eggNOG; arCOG01904; Archaea.
DR HOGENOM; CLU_088476_0_0_2; -.
DR OrthoDB; 30955at2157; -.
DR UniPathway; UPA00276; UER00929.
DR Proteomes; UP000007478; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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; 2.40.30.30; Riboflavin kinase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_01285; Riboflavin_kinase; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR000835; HTH_MarR-typ.
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; RIBOFLAVIN KINASE; 1.
DR PANTHER; PTHR40706:SF1; RIBOFLAVIN KINASE; 1.
DR Pfam; PF01982; CTP-dep_RFKase; 1.
DR Pfam; PF13412; HTH_24; 1.
DR SMART; SM00347; HTH_MARR; 1.
DR SUPFAM; SSF82114; Riboflavin kinase-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01285};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01285};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01285};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01285};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01285}; Reference proteome {ECO:0000313|Proteomes:UP000007478};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01285}.
FT DOMAIN 1..101
FT /note="HTH marR-type"
FT /evidence="ECO:0000259|SMART:SM00347"
FT BINDING 95..100
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
FT BINDING 178
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
FT BINDING 186
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
FT BINDING 191..194
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
SQ SEQUENCE 211 AA; 23971 MW; 873BD7956AB6D384 CRC64;
MKKLKLILQI AKNGAIGEKV KITLRELSRE LEVSPQTVLR WLDELEKEGY ITRTVEGKKT
CIELTDKALM YLEELYEQLS NVLYQGVIIG EVISGLGEGA YYVRQYAPLI REYLGFEPYP
GTLNIKIIFP KTIFDALCNV KPILIPGFVK NGRTFGDVRA YKVKINGIEG AIVIPSRTIH
PPRIAEVIAP IYLRRELNLK DGSRIKLKVI R
//
