RIFK_YEAST
ID RIFK_YEAST Reviewed; 218 AA.
AC Q03778; D6VSL7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Riboflavin kinase;
DE EC=2.7.1.26 {ECO:0000269|PubMed:10887197};
DE AltName: Full=Flavin mononucleotide kinase 1;
DE Flags: Precursor;
GN Name=FMN1; OrderedLocusNames=YDR236C; ORFNames=YD8419.03C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=10887197; DOI=10.1074/jbc.m004621200;
RA Santos M.A., Jimenez A., Revuelta J.L.;
RT "Molecular characterization of FMN1, the structural gene for the
RT monofunctional flavokinase of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:28618-28624(2000).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to
CC form flavin mononucleotide (FMN) coenzyme.
CC {ECO:0000269|PubMed:10887197}.
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 Evidence={ECO:0000269|PubMed:10887197};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14358;
CC Evidence={ECO:0000305|PubMed:10887197};
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 -!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:10887197}.
CC Mitochondrion inner membrane {ECO:0000269|PubMed:10887197}. Endoplasmic
CC reticulum {ECO:0000305}. Note=90% microsomal. 10% mitochondrial. Found
CC to be present in the inner membrane of mitochondria. The C-terminus is
CC located in the matrix.
CC -!- MISCELLANEOUS: FMN1 is essential for growth on rich medium.
CC -!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the flavokinase family. {ECO:0000305}.
CC -!- CAUTION: The subcellular location of this enzyme needs further
CC confirmation. {ECO:0000305}.
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DR EMBL; Z49701; CAA89722.1; -; Genomic_DNA.
DR EMBL; AY557733; AAS56059.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12077.1; -; Genomic_DNA.
DR PIR; S54532; S54532.
DR RefSeq; NP_010522.1; NM_001180544.1.
DR AlphaFoldDB; Q03778; -.
DR SMR; Q03778; -.
DR BioGRID; 32287; 206.
DR DIP; DIP-1316N; -.
DR IntAct; Q03778; 1.
DR MINT; Q03778; -.
DR STRING; 4932.YDR236C; -.
DR iPTMnet; Q03778; -.
DR MaxQB; Q03778; -.
DR PaxDb; Q03778; -.
DR PRIDE; Q03778; -.
DR EnsemblFungi; YDR236C_mRNA; YDR236C; YDR236C.
DR GeneID; 851822; -.
DR KEGG; sce:YDR236C; -.
DR SGD; S000002644; FMN1.
DR VEuPathDB; FungiDB:YDR236C; -.
DR eggNOG; KOG3110; Eukaryota.
DR GeneTree; ENSGT00390000015537; -.
DR HOGENOM; CLU_048437_3_2_1; -.
DR InParanoid; Q03778; -.
DR OMA; EVYKMVL; -.
DR BioCyc; MetaCyc:YDR236C-MON; -.
DR BioCyc; YEAST:YDR236C-MON; -.
DR Reactome; R-SCE-196843; Vitamin B2 (riboflavin) metabolism.
DR UniPathway; UPA00276; UER00406.
DR PRO; PR:Q03778; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03778; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0009398; P:FMN biosynthetic process; IDA:SGD.
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 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Flavoprotein; FMN; Kinase; Magnesium;
KW Membrane; Metal-binding; Microsome; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Signal; Transferase; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..218
FT /note="Riboflavin kinase"
FT /id="PRO_0000030437"
FT ACT_SITE 155
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q969G6"
FT BINDING 74
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q969G6"
SQ SEQUENCE 218 AA; 24537 MW; D96995F4F2EBC9F4 CRC64;
MFTWTIYVSL LLVLAGTFLM NRNTNTDIID TFKREVDLPI PAQPGPPFPL VTDYCDIVCG
FGRGSAELGI PTANVPINQL PKGINDLDLG VYFGFAHIKT VDGQELSVET RRDGRTVVYN
YGQYLSEAND DLSVLPMVLS VGKNPFYGND FKTMELHIIH DFKNDFYGAR VKFNILGHIR
PELNYTTKEA LIEDINIDIR TAQTVLATPP YQVFKQQL
