RIFK_YARLI
ID RIFK_YARLI Reviewed; 192 AA.
AC Q6CG11;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Riboflavin kinase;
DE EC=2.7.1.26;
DE AltName: Full=Flavin mononucleotide kinase 1;
GN Name=FMN1; OrderedLocusNames=YALI0B01826g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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}.
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DR EMBL; CR382128; CAG82619.1; -; Genomic_DNA.
DR RefSeq; XP_500401.1; XM_500401.1.
DR AlphaFoldDB; Q6CG11; -.
DR SMR; Q6CG11; -.
DR STRING; 4952.CAG82619; -.
DR EnsemblFungi; CAG82619; CAG82619; YALI0_B01826g.
DR GeneID; 2907158; -.
DR KEGG; yli:YALI0B01826g; -.
DR VEuPathDB; FungiDB:YALI0_B01826g; -.
DR HOGENOM; CLU_048437_3_2_1; -.
DR InParanoid; Q6CG11; -.
DR OMA; EVYKMVL; -.
DR UniPathway; UPA00276; UER00406.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:EnsemblFungi.
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..192
FT /note="Riboflavin kinase"
FT /id="PRO_0000301850"
FT ACT_SITE 129
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q969G6"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q969G6"
SQ SEQUENCE 192 AA; 21820 MW; FC62F8024FB22660 CRC64;
MMISCTRTAI LPLRRRLMTA STAYPIKFAS SIIPGYGRGS ADLGIPTANI PIDDVPVLDA
LDTGIYYGLV QILKTDKPSE KKTSEFQKDR VVDFQYTNKL NDQEINAVLP MVMSVGWNPF
YKNDQKSAEI HIIHKFAHTF YGASIKVMVL GYLRPEKNFT SLEALVDEIH NDIKVSEEKM
EGTREKKDQF WQ
