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RIFK_NEUCR
ID   RIFK_NEUCR              Reviewed;         237 AA.
AC   Q6M923; Q7RZ99;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Riboflavin kinase;
DE            EC=2.7.1.26;
DE   AltName: Full=Flavin mononucleotide kinase 1;
GN   Name=fmn1; ORFNames=G17A4.020, NCU03970, NCU20237;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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=CAF06137.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; BX908812; CAF06137.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002241; EAA28373.1; -; Genomic_DNA.
DR   RefSeq; XP_957609.1; XM_952516.2.
DR   AlphaFoldDB; Q6M923; -.
DR   SMR; Q6M923; -.
DR   STRING; 5141.EFNCRP00000003538; -.
DR   EnsemblFungi; EAA28373; EAA28373; NCU03970.
DR   GeneID; 3873731; -.
DR   KEGG; ncr:NCU03970; -.
DR   VEuPathDB; FungiDB:NCU03970; -.
DR   HOGENOM; CLU_048437_3_2_1; -.
DR   InParanoid; Q6M923; -.
DR   OMA; KFHKLPD; -.
DR   UniPathway; UPA00276; UER00406.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
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; -; 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..237
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000301846"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        158
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q969G6"
FT   BINDING         48
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q969G6"
SQ   SEQUENCE   237 AA;  26542 MW;  FB626DCA91BB9384 CRC64;
     MSLPNPDNRP LLIGPPTGPE APFPFRMEGE VISGFGRGSK ELGIPTANLP VDDENAWIKN
     IDSGIYFGWA SLKLPASHPN SVLYQKPPTS EPVMMDPVQQ QQQQQQQQRN QQQQQEGGVG
     SAQQEKLVDQ ETGQWQIYPM VMSIGYNPFY KNTVRSAEVH VLGEFAADFY GVGMRLLITG
     FIRNEKDYSG LEALIADIHF DCEVARHSLA RKGWRVRELG VKEGEEEGEL DGSWLVR
 
 
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