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RIFK_AERPE
ID   RIFK_AERPE              Reviewed;         132 AA.
AC   Q9YA27;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Riboflavin kinase {ECO:0000255|HAMAP-Rule:MF_01285};
DE            Short=RFK {ECO:0000255|HAMAP-Rule:MF_01285};
DE            EC=2.7.1.161 {ECO:0000255|HAMAP-Rule:MF_01285};
DE   AltName: Full=CTP-dependent riboflavin kinase {ECO:0000255|HAMAP-Rule:MF_01285};
DE   AltName: Full=CTP:riboflavin 5'-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01285};
DE   AltName: Full=Flavokinase {ECO:0000255|HAMAP-Rule:MF_01285};
GN   Name=ribK {ECO:0000255|HAMAP-Rule:MF_01285}; OrderedLocusNames=APE_2112.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of riboflavin
CC       (vitamin B2) to form flavin mononucleotide (FMN). {ECO:0000255|HAMAP-
CC       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:0000255|HAMAP-Rule:MF_01285};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01285};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01285};
CC   -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC       (CTP route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01285}.
CC   -!- SIMILARITY: Belongs to the archaeal riboflavin kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01285}.
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DR   EMBL; BA000002; BAA81123.2; -; Genomic_DNA.
DR   PIR; C72517; C72517.
DR   AlphaFoldDB; Q9YA27; -.
DR   SMR; Q9YA27; -.
DR   STRING; 272557.APE_2112.1; -.
DR   DNASU; 1445199; -.
DR   EnsemblBacteria; BAA81123; BAA81123; APE_2112.1.
DR   KEGG; ape:APE_2112.1; -.
DR   eggNOG; arCOG01904; Archaea.
DR   OMA; PYEGTLN; -.
DR   UniPathway; UPA00276; UER00929.
DR   Proteomes; UP000002518; 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; 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   PANTHER; PTHR40706; PTHR40706; 1.
DR   Pfam; PF01982; CTP-dep_RFKase; 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..132
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000322065"
FT   BINDING         13..18
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT   BINDING         98
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT   BINDING         106
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
FT   BINDING         111..114
FT                   /ligand="CDP"
FT                   /ligand_id="ChEBI:CHEBI:58069"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01285"
SQ   SEQUENCE   132 AA;  14456 MW;  992AB143E6CF1D05 CRC64;
     MDCGVFEGTV FSGLGHGSFY VSIYARNLRR ALGYTPYPGT LNLRVGDAAE RLAGCIERAR
     GVRIEPPPIP GERLASVLAF PVEIEGGVRG HIVRPEITVY KGDVVEIVAD VYLRDVLKIS
     DGDKVRFRLL DP
 
 
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