ID RIFK_CHAGB Reviewed; 235 AA. AC P0C5D9; Q2GSA5; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 22-FEB-2023, entry version 71. DE RecName: Full=Riboflavin kinase; DE EC=2.7.1.26; DE AltName: Full=Flavin mononucleotide kinase 1; GN Name=FMN1; ORFNames=CHGG_09149.2; OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / OS NRRL 1970) (Soil fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium. OX NCBI_TaxID=306901; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970; RX PubMed=25720678; DOI=10.1128/genomea.00021-15; RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.; RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum."; RL Genome Announc. 3:E0002115-E0002115(2015). 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=EAQ85135.1; Type=Erroneous gene model prediction; Note=The predicted gene CHGG_09149 has been split into 2 genes: CHGG_09149.1 and CHGG_09149.2.; 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; CH408034; EAQ85135.1; ALT_SEQ; Genomic_DNA. DR RefSeq; XP_001227076.1; XM_001227075.1. DR AlphaFoldDB; P0C5D9; -. DR SMR; P0C5D9; -. DR STRING; 306901.P0C5D9; -. DR GeneID; 4395860; -. DR VEuPathDB; FungiDB:CHGG_09149; -. DR eggNOG; KOG3110; Eukaryota. DR eggNOG; KOG4039; Eukaryota. DR HOGENOM; CLU_599913_0_0_1; -. DR InParanoid; P0C5D9; -. DR OrthoDB; 24906at2759; -. DR UniPathway; UPA00276; UER00406. DR Proteomes; UP000001056; 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; 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..235 FT /note="Riboflavin kinase" FT /id="PRO_0000301839" FT ACT_SITE 140 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT BINDING 45 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q969G6" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q969G6" SQ SEQUENCE 235 AA; 24680 MW; 90586511CDB868EF CRC64; MAHQPPNRPP LIGDPSGPAP PYPFRMSGLV ISGFGRGSKE LGIPTANLPV DDAQTPWISS IPSGVYFGWA SLNLPASHPD SLTSSAAAAA AAAAAAAAPG EDGGGAGEQR QRGGNGFAVY PMVMSIGYNP FYKNTVRSAE VHVLHRFGAD FYGVEMRLLI AGFIREEKDY SGLEALIADI EFDCEVAKRS LAREGWAPSG VDVEVDVPGE GVKVLRGSLE CGWLIRPDEL GEGGK //