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Reviewed, UniProtKB/Swiss-Prot O74866 (RIFK_SCHPO)

Last modified June 16, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Riboflavin kinase
    EC=2.7.1.26
Alternative name(s):
    Flavin mononucleotide kinase 1
    ATP:riboflavin 5'-phosphotransferase
    Flavokinase
Gene names
Name: fmn1
ORF Names: SPCC18.16c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Binds 1 zinc ion per subunit.

Pathway

Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.

Subunit structure

Monomer.

Sequence similarities

Belongs to the flavokinase family.

Ontologies

Keywords
   LigandATP-binding
FMN
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processriboflavin biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_SPombe

nucleus

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

riboflavin kinase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 163163Riboflavin kinase
PRO_0000194151

Sites

Active site961Nucleophile Probable
Metal binding451Zinc

Secondary structure

........................ 163
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O74866-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: ADFD49D12FD7472F

FASTA16318,913
        10         20         30         40         50         60 
MTVNLEEKRP EIVGPEKVQS PYPIRFEGKV VHGFGRGSKE LGIPTANISE DAIQELLRYR 

        70         80         90        100        110        120 
DSGVYFGYAM VQKRVFPMVM SVGWNPYYKN KLRSAEVHLI ERQGEDFYEE IMRVIVLGYI 

       130        140        150        160 
RPELNYAGLD KLIEDIHTDI RVALNSMDRP SYSSYKKDPF FKV 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold."
Bauer S., Kemter K., Bacher A., Huber R., Fischer M., Steinbacher S.
J. Mol. Biol. 326:1463-1473(2003) [PubMed: 12595258] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Cross-references

Sequence databases

CU329672 Genomic DNA. Translation: CAA21430.1.
PIRT41159.
RefSeqNP_588395.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1N05X-ray2.10A1-163[»]
1N06X-ray2.00A/B1-163[»]
1N07X-ray2.45A/B1-163[»]
1N08X-ray1.60A/B1-163[»]
ModBaseSearch...

Genome annotation databases

GeneID2539192.
KEGGspo:SPCC18.16c.
NMPDRfig|4896.1.peg.733.

Organism-specific databases

GeneDB_SpombeSPCC18.16c.

Phylogenomic databases

OMAO74866. METHVIH.

Enzyme and pathway databases

BRENDA2.7.1.26. 653.

Gene expression databases

ArrayExpressO74866.

Family and domain databases

InterProIPR015865. Riboflavin_kinase.
[Graphical view]
Gene3DG3DSA:2.40.30.30. Riboflavin_kinase. 1 hit.
PANTHERPTHR22749. Riboflavin_kinase. 1 hit.
PfamPF01687. Flavokinase. 1 hit.
[Graphical view]
ProDomPD003662. FAD_Synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameRIFK_SCHPO
AccessionPrimary (citable) accession number: O74866
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: November 1, 1998
Last modified: June 16, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents