ID   RIFK_ASHGO              Reviewed;         186 AA.
AC   Q75DY2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Riboflavin kinase;
DE            EC=2.7.1.26;
DE   AltName: Full=Flavin mononucleotide kinase 1;
GN   Name=FMN1; OrderedLocusNames=ABL109W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS50662.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016815; AAS50662.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_982838.1; NM_208191.1.
DR   AlphaFoldDB; Q75DY2; -.
DR   SMR; Q75DY2; -.
DR   STRING; 33169.AAS50662; -.
DR   GeneID; 4618918; -.
DR   KEGG; ago:AGOS_ABL109W; -.
DR   eggNOG; KOG3110; Eukaryota.
DR   InParanoid; Q75DY2; -.
DR   UniPathway; UPA00276; UER00406.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0009398; P:FMN biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR   GO; GO:0006771; P:riboflavin metabolic process; IBA:GO_Central.
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..186
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000301832"
FT   ACT_SITE        123
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q969G6"
FT   BINDING         44
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q969G6"
SQ   SEQUENCE   186 AA;  20984 MW;  DA16FB2E83EF3A9E CRC64;
     MARRPVDIPI PASPVQPFPI LTEYVDIVAG FGRGSAELGI PTANVPIEQL PSEVNEMATG
     VYFGWARLRP NMDQEAQVHH RNDGSEVIYN FGSKLSETER GVFPIVLSVG WNPFYNNSKK
     TVELHILNDF EEDFYGAKIK FSFLGYIRPE LNYTTKEALI EDIHTDIKIA SEVLHTEPYS
     SLKNQL