RIFK_THEAC
ID RIFK_THEAC Reviewed; 220 AA.
AC Q9HJA6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=Ta1064;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445066; CAC12192.1; -; Genomic_DNA.
DR RefSeq; WP_010901475.1; NC_002578.1.
DR PDB; 3CTA; X-ray; 2.20 A; A=2-220.
DR PDB; 5TRD; X-ray; 1.85 A; A/B=2-220.
DR PDBsum; 3CTA; -.
DR PDBsum; 5TRD; -.
DR AlphaFoldDB; Q9HJA6; -.
DR SMR; Q9HJA6; -.
DR STRING; 273075.Ta1064; -.
DR EnsemblBacteria; CAC12192; CAC12192; CAC12192.
DR GeneID; 1456578; -.
DR KEGG; tac:Ta1064; -.
DR eggNOG; arCOG01904; Archaea.
DR HOGENOM; CLU_088476_0_0_2; -.
DR OMA; AYYVRQY; -.
DR OrthoDB; 91297at2157; -.
DR BRENDA; 2.7.1.161; 6324.
DR UniPathway; UPA00276; UER00929.
DR EvolutionaryTrace; Q9HJA6; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008531; F:riboflavin kinase activity; IEA:InterPro.
DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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 InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR039063; RibK_CTP-dep.
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 Pfam; PF13545; HTH_Crp_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF82114; SSF82114; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..220
FT /note="Riboflavin kinase"
FT /id="PRO_0000322106"
FT REGION 1..92
FT /note="H-T-H motif-like"
FT REGION 93..220
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 195
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 200..203
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000250"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:5TRD"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:5TRD"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:5TRD"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:5TRD"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:5TRD"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:5TRD"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:5TRD"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:5TRD"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:5TRD"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:5TRD"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:5TRD"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:5TRD"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5TRD"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:5TRD"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5TRD"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:5TRD"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:5TRD"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:5TRD"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:5TRD"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:5TRD"
SQ SEQUENCE 220 AA; 24997 MW; BB0F694447629612 CRC64;
METDDQYYRA IKKIKEAAEA SNRAYLTSSK LADMLGISQQ SASRIIIDLE KNGYITRTVT
KRGQILNITE KGLDVLYTEF ADLSRILAIK NNVVITGTVT SGMGEGRYYV ARKQYIIQFQ
EKLGIIPYLG TLNIKVDQAS LPELRKIRGF RGIHIEGFKT EDRTFGSVKA FPAKIQNIPC
FVIMPERTVY TDVIEIISDK YLREEINLHD GDRVSVEVYT
