ID   RIFK_LODEL              Reviewed;         182 AA.
AC   A5E1A0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Riboflavin kinase;
DE            EC=2.7.1.26;
DE   AltName: Full=Flavin mononucleotide kinase 1;
GN   Name=FMN1; ORFNames=LELG_03387;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to
CC       form flavin mononucleotide (FMN) coenzyme. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Zinc or magnesium. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC       (ATP route): step 1/1.
CC   -!- SIMILARITY: Belongs to the flavokinase family. {ECO:0000305}.
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DR   EMBL; CH981527; EDK45208.1; -; Genomic_DNA.
DR   RefSeq; XP_001525459.1; XM_001525409.1.
DR   AlphaFoldDB; A5E1A0; -.
DR   SMR; A5E1A0; -.
DR   STRING; 379508.A5E1A0; -.
DR   EnsemblFungi; EDK45208; EDK45208; LELG_03387.
DR   GeneID; 5232703; -.
DR   KEGG; lel:LELG_03387; -.
DR   VEuPathDB; FungiDB:LELG_03387; -.
DR   eggNOG; KOG3110; Eukaryota.
DR   HOGENOM; CLU_048437_3_2_1; -.
DR   InParanoid; A5E1A0; -.
DR   OMA; EVYKMVL; -.
DR   OrthoDB; 1534271at2759; -.
DR   UniPathway; UPA00276; UER00406.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway.
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   InterPro; IPR023468; Riboflavin_kinase.
DR   InterPro; IPR015865; Riboflavin_kinase_bac/euk.
DR   InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR   PANTHER; PTHR22749; PTHR22749; 1.
DR   Pfam; PF01687; Flavokinase; 1.
DR   SMART; SM00904; Flavokinase; 1.
DR   SUPFAM; SSF82114; SSF82114; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Flavoprotein; FMN; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..182
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000301843"
FT   ACT_SITE        117
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q969G6"
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q969G6"
SQ   SEQUENCE   182 AA;  20838 MW;  4918FA4FA3A74FE8 CRC64;
     MTRPETIIPE KPTSPYPIHT TAPIISGFGR GSSELGIPTA NIPINAQLNS LPTGIYYGWC
     KIHPVSDQND ETRTRPDGQL ILFNHGNKLQ ANELVVHPMV MSIGWNPFYQ NKEKAAEIHI
     MSKFERDFYG AELEFIVLGY VRPELDYTTK EALIEDILTD IRISRDILEN KEEYTKYKKE
     LE