RIFK_CANGA
ID RIFK_CANGA Reviewed; 189 AA.
AC Q6FM49;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Riboflavin kinase;
DE EC=2.7.1.26;
DE AltName: Full=Flavin mononucleotide kinase 1;
GN Name=FMN1; OrderedLocusNames=CAGL0K11022g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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=CAG61658.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR380957; CAG61658.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_448695.1; XM_448695.1.
DR AlphaFoldDB; Q6FM49; -.
DR SMR; Q6FM49; -.
DR STRING; 5478.XP_448695.1; -.
DR EnsemblFungi; CAG61658; CAG61658; CAGL0K11022g.
DR GeneID; 2890083; -.
DR KEGG; cgr:CAGL0K11022g; -.
DR eggNOG; KOG3110; Eukaryota.
DR HOGENOM; CLU_048437_3_2_1; -.
DR InParanoid; Q6FM49; -.
DR UniPathway; UPA00276; UER00406.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:EnsemblFungi.
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..189
FT /note="Riboflavin kinase"
FT /id="PRO_0000301838"
FT ACT_SITE 124
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q969G6"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q969G6"
SQ SEQUENCE 189 AA; 21196 MW; F7A85F00F5ACB876 CRC64;
MTVRDVDVPI PEQPGAPYPI VTKCCDIVCG FGRGSSELGI PTANVPVDQL PEVVNKLELG
VYFGYAKVTP VAHDLEQVER EDGRVVSYNY GSHLEEDNGD LEVLPVVLSV GKNPFYHNDF
KTVEIHILHD FKSTFYGAKI KFNILGYVRP ELDYTSKEAL IEDIKTDIEI SKQVLDTEPY
RAHMAELLK
