Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9Y7P0 (RISA_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Riboflavin synthase

Short name=RS
EC=2.5.1.9
Gene names
Name:rib5
ORF Names:SPCC1450.13c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil. Ref.1

Catalytic activity

2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine.

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.

Subunit structure

Homotrimer. Ref.1

Sequence similarities

Contains 2 lumazine-binding repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208Riboflavin synthase
PRO_0000068173

Regions

Repeat1 – 9797Lumazine-binding 1
Repeat98 – 19598Lumazine-binding 2
Region81 – 855Lumazine binding Probable
Region179 – 1835Lumazine binding Probable

Secondary structure

......................................... 208
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y7P0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 59C5065DDD4C7B8B

FASTA20822,861
        10         20         30         40         50         60 
MFTGLVEAIG VVKDVQGTID NGFAMKIEAP QILDDCHTGD SIAVNGTCLT VTDFDRYHFT 

        70         80         90        100        110        120 
VGIAPESLRL TNLGQCKAGD PVNLERAVLS STRMGGHFVQ GHVDTVAEIV EKKQDGEAID 

       130        140        150        160        170        180 
FTFRPRDPFV LKYIVYKGYI ALDGTSLTIT HVDDSTFSIM MISYTQSKVI MAKKNVGDLV 

       190        200 
NVEVDQIGKY TEKLVEAHIA DWIKKTQA 

« Hide

References

« Hide 'large scale' references
[1]"Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments."
Fischer M., Schott A.-K., Kemter K., Feicht R., Richter G., Illarionov B., Eisenreich W., Gerhardt S., Cushman M., Steinbacher S., Huber R., Bacher A.
BMC Biochem. 4:18-18(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine."
Gerhardt S., Schott A.-K., Kairies N., Cushman M., Illarionov B., Eisenreich W., Bacher A., Huber R., Steinbacher S., Fischer M.
Structure 10:1371-1381(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF505789 mRNA. Translation: AAM28201.1.
CU329672 Genomic DNA. Translation: CAB40180.1.
PIRT40995.
RefSeqNP_588312.1. NM_001023302.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KZLX-ray2.10A1-208[»]
ProteinModelPortalQ9Y7P0.
SMRQ9Y7P0. Positions 1-202.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPCC1450.13c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1450.13c.1; SPCC1450.13c.1:pep; SPCC1450.13c.
GeneID2539183.
KEGGspo:SPCC1450.13c.

Organism-specific databases

PomBaseSPCC1450.13c.

Phylogenomic databases

eggNOGCOG0307.
HOGENOMHOG000151757.
KOK00793.
OMASRYVVEK.
OrthoDBEOG4KSSV0.

Enzyme and pathway databases

BRENDA2.5.1.9. 5615.
UniPathwayUPA00275; UER00405.

Family and domain databases

Gene3D2.40.30.20. 2 hits.
InterProIPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERPTHR21098. PTHR21098. 1 hit.
PfamPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 2 hits.
TIGRFAMsTIGR00187. ribE. 1 hit.
PROSITEPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y7P0.
NextBio20800354.

Entry information

Entry nameRISA_SCHPO
AccessionPrimary (citable) accession number: Q9Y7P0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1999
Last modified: May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families