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   03-AUG-2022, entry version 68.
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};
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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   EnsemblFungi; EAQ85135; EAQ85135; CHGG_09149.
DR   GeneID; 4395860; -.
DR   eggNOG; KOG3110; Eukaryota.
DR   eggNOG; KOG4039; Eukaryota.
DR   HOGENOM; CLU_599913_0_0_1; -.
DR   InParanoid; P0C5D9; -.
DR   OrthoDB; 1601023at2759; -.
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; -; 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..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