Q03778 (RIFK_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Riboflavin kinase
EC=2.7.1.26

Alternative name(s):
Flavin mononucleotide kinase 1

Gene names

Name:	FMN1
Ordered Locus Names:	YDR236C
ORF Names:	YD8419.03C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Catalytic activity	ATP + riboflavin = ADP + FMN.
Cofactor	Zinc or magnesium By similarity.
Pathway	Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
Subcellular location	Microsome. Mitochondrion inner membrane. Endoplasmic reticulum Potential. Note: 90% microsomal. 10% mitochondrial. Found to be present in the inner membrane of mitochondria. The C-terminus is located in the matrix. Ref.4
Miscellaneous	FMN1 is essential for growth on rich medium. Present with 830 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the flavokinase family.
Caution	The subcellular location of this enzyme needs further confirmation.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome Mitochondrion Mitochondrion inner membrane
Domain	Signal
Ligand	ATP-binding FMN Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	FMN biosynthetic process Inferred from direct assay Ref.4. Source: SGD riboflavin biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from direct assay Ref.4. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW riboflavin kinase activity Inferred from direct assay PubMed 12614612. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 218	199	Riboflavin kinase		PRO_0000030437
Sites
	Active site	155	1	Nucleophile By similarity
	Metal binding	72	1	Magnesium or zinc By similarity
Amino acid modifications
	Modified residue	147	1	Phosphotyrosine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q03778 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D96995F4F2EBC9F4	FASTA	218	24,537
	10 20 30 40 50 60 MFTWTIYVSL LLVLAGTFLM NRNTNTDIID TFKREVDLPI PAQPGPPFPL VTDYCDIVCG 70 80 90 100 110 120 FGRGSAELGI PTANVPINQL PKGINDLDLG VYFGFAHIKT VDGQELSVET RRDGRTVVYN 130 140 150 160 170 180 YGQYLSEAND DLSVLPMVLS VGKNPFYGND FKTMELHIIH DFKNDFYGAR VKFNILGHIR 190 200 210 PELNYTTKEA LIEDINIDIR TAQTVLATPP YQVFKQQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Molecular characterization of FMN1, the structural gene for the monofunctional flavokinase of Saccharomyces cerevisiae." Santos M.A., Jimenez A., Revuelta J.L. J. Biol. Chem. 275:28618-28624(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z49701 Genomic DNA. Translation: CAA89722.1. AY557733 Genomic DNA. Translation: AAS56059.1. BK006938 Genomic DNA. Translation: DAA12077.1.
PIR	S54532.
RefSeq	NP_010522.1. NM_001180544.1.
3D structure databases
ProteinModelPortal	Q03778.
SMR	Q03778. Positions 57-216.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1316N.
IntAct	Q03778. 1 interaction.
MINT	MINT-406034.
STRING	4932.YDR236C.
Proteomic databases
PaxDb	Q03778.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR236C; YDR236C; YDR236C.
GeneID	851822.
KEGG	sce:YDR236C.
Organism-specific databases
CYGD	YDR236c.
SGD	S000002644. FMN1.
Phylogenomic databases
eggNOG	COG0196.
GeneTree	ENSGT00390000015537.
HOGENOM	HOG000260803.
KO	K00861.
OMA	CDIVCGF.
OrthoDB	EOG4BCHXC.
Enzyme and pathway databases
BioCyc	MetaCyc:YDR236C-MONOMER.
UniPathway	UPA00276; UER00406.
Gene expression databases
Genevestigator	Q03778.
GermOnline	YDR236C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.40.30.30. 1 hit.
InterPro	IPR023468. Riboflavin_kinase. IPR015865. Riboflavin_kinase_bac/euk. IPR023465. Riboflavin_kinase_domain. [Graphical view]
PANTHER	PTHR22749. PTHR22749. 1 hit.
Pfam	PF01687. Flavokinase. 1 hit. [Graphical view]
SMART	SM00904. Flavokinase. 1 hit. [Graphical view]
SUPFAM	SSF82114. Riboflavin_kinase. 1 hit.
ProtoNet	Search...
Other
NextBio	969695.

Entry information

Entry name

RIFK_YEAST

Accession

Primary (citable) accession number: Q03778
Secondary accession number(s): D6VSL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program