ID RIFK_EMENI Reviewed; 210 AA. AC Q5AW61; C8VBE5; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 02-SEP-2026, entry version 106. DE RecName: Full=Riboflavin kinase; DE EC=2.7.1.26; DE AltName: Full=Flavin mononucleotide kinase 1; GN Name=fmn1; ORFNames=AN7469; OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / OS M139) (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Nidulantes. OX NCBI_TaxID=227321; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). RN [2] RP GENOME REANNOTATION. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003; RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K., RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J., RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., RA Oliver S.G., Turner G.; RT "The 2008 update of the Aspergillus nidulans genome annotation: a community RT effort."; RL Fungal Genet. Biol. 46:S2-13(2009). CC -!- FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to CC form flavin mononucleotide (FMN) coenzyme. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=riboflavin + ATP = FMN + ADP + 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 --------------------------------------------------------------------------- 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; AACD01000129; EAA62049.1; -; Genomic_DNA. DR EMBL; BN001304; CBF79442.1; -; Genomic_DNA. DR RefSeq; XP_680738.1; XM_675646.1. DR AlphaFoldDB; Q5AW61; -. DR SMR; Q5AW61; -. DR FunCoup; Q5AW61; 364. DR STRING; 227321.Q5AW61; -. DR EnsemblFungi; CBF79442; CBF79442; ANIA_07469. DR GeneID; 2869537; -. DR KEGG; ani:ANIA_07469; -. DR eggNOG; KOG3110; Eukaryota. DR HOGENOM; CLU_048437_3_2_1; -. DR InParanoid; Q5AW61; -. DR OMA; FDCEVAR; -. DR OrthoDB; 276388at2759; -. DR UniPathway; UPA00276; UER00406. DR Proteomes; UP000000560; Chromosome IV. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-EC. DR GO; GO:0009398; P:FMN biosynthetic process; IBA:GO_Central. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro. DR GO; GO:0006771; P:riboflavin metabolic process; IBA:GO_Central. DR FunFam; 2.40.30.30:FF:000008; Riboflavin kinase; 1. 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..210 FT /note="Riboflavin kinase" FT /id="PRO_0000301841" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..11 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 113 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT BINDING 44 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q969G6" FT BINDING 46 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q969G6" SQ SEQUENCE 210 AA; 22916 MW; CFA2B4DD973852A4 CRC64; MRPSNPRPPV TGPDSGPEAP FPIRLSGPVI KGFGRGSKEL GIPTANIPVD GLEEVLPKEL GVGVYYGVVA LDPATAPAPS SSDSTSGDAA PILPAVLSIG YNPYYKNKTR SIEIHIMPSL TLPSPTAPSE EKEKVKFHKL PDFYGTKLNL LMLGYIRPEY DYVSMEALVE DIRIDCEVAR ASLLRPAYRV YLDGNEDETV SAQRDWLRSF //