ID   RIFK_NEOFI              Reviewed;         218 AA.
AC   A1DG00;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Riboflavin kinase;
DE            EC=2.7.1.26;
DE   AltName: Full=Flavin mononucleotide kinase 1;
GN   Name=fmn1; ORFNames=NFIA_082540;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR   EMBL; DS027696; EAW18307.1; -; Genomic_DNA.
DR   RefSeq; XP_001260204.1; XM_001260203.1.
DR   AlphaFoldDB; A1DG00; -.
DR   SMR; A1DG00; -.
DR   STRING; 36630.CADNFIAP00006812; -.
DR   EnsemblFungi; EAW18307; EAW18307; NFIA_082540.
DR   GeneID; 4586761; -.
DR   KEGG; nfi:NFIA_082540; -.
DR   VEuPathDB; FungiDB:NFIA_082540; -.
DR   eggNOG; KOG3110; Eukaryota.
DR   HOGENOM; CLU_048437_3_2_1; -.
DR   OMA; KFHKLPD; -.
DR   OrthoDB; 1534271at2759; -.
DR   UniPathway; UPA00276; UER00406.
DR   Proteomes; UP000006702; 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..218
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000301845"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        120
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   218 AA;  23563 MW;  F670445E67236D81 CRC64;
     MRPDGPRDPV AGPDSGPEPP YPVRLSGPVI KGFGRGSKEL GIPTANIPAE GLAEYPDLQV
     GVYYGVVALD PAKFQYQEDQ GEGSTSSTGG AGAGAGAAIL PAVLSIGYNP FYKNKTKSIE
     IHIMPPLSSP SPTAEGAGEV KFHKLPDFYG TQLKLLILGY IRPEYDYVSL EALIEDIRVD
     CEVARKSLQR PAYACYIDGD EKECSDAVRE QRRWLVNF