ID RIFK_EREGS Reviewed; 186 AA. AC Q75DY2; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 24-JAN-2024, entry version 104. DE RecName: Full=Riboflavin kinase; DE EC=2.7.1.26; DE AltName: Full=Flavin mononucleotide kinase 1; GN Name=FMN1; OrderedLocusNames=ABL109W; OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Ashbya 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; 284811.Q75DY2; -. DR GeneID; 4618918; -. DR KEGG; ago:AGOS_ABL109W; -. DR eggNOG; KOG3110; Eukaryota. DR InParanoid; Q75DY2; -. DR OrthoDB; 24906at2759; -. 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; Riboflavin kinase-like; 1. DR InterPro; IPR023468; Riboflavin_kinase. DR InterPro; IPR015865; Riboflavin_kinase_bac/euk. DR InterPro; IPR023465; Riboflavin_kinase_dom_sf. DR PANTHER; PTHR22749:SF6; RIBOFLAVIN KINASE; 1. DR PANTHER; PTHR22749; RIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE; 1. DR Pfam; PF01687; Flavokinase; 1. DR SMART; SM00904; Flavokinase; 1. DR SUPFAM; SSF82114; Riboflavin kinase-like; 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 //