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P38145 (RISA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 111. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Ordered Locus Names:YBR256C
ORF Names:YBR1724
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length238 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 By similarity.

Miscellaneous

Present with 7300 molecules/cell in log phase SD medium.

Sequence similarities

Contains 2 lumazine-binding repeats.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   DomainRepeat
   Molecular functionTransferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processriboflavin biosynthetic process

Inferred from mutant phenotype Ref.1. Source: SGD

   Molecular_functionoxidoreductase activity

Inferred from electronic annotation. Source: InterPro

riboflavin synthase activity

Inferred from direct assay Ref.1. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-2083267,EBI-2083267
ARO8P530901EBI-2083267,EBI-2042933
IPP1P008171EBI-2083267,EBI-9338
RNR1P215241EBI-2083267,EBI-15234
VAS1P07806-11EBI-2083267,EBI-1009942From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 238238Riboflavin synthase
PRO_0000068174

Regions

Repeat1 – 103103Lumazine-binding 1
Repeat104 – 205102Lumazine-binding 2
Region87 – 915Lumazine binding Probable
Region189 – 1935Lumazine binding Probable

Amino acid modifications

Modified residue951Phosphoserine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P38145 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: EA57EAD542D46897

FASTA23826,196
        10         20         30         40         50         60 
MFTGIVECMG TVLENNPYDD SESGGQGVSI TIGNAGSILT DCHVGDSIAV NGVCLTVTEF 

        70         80         90        100        110        120 
NNDSFKVGIS PETIKRSNVA SWIQGTQVNL ERAVSQDVRF GGHYVQGHVD TVANIVSRRP 

       130        140        150        160        170        180 
EGNSIIFGFQ LRDQEYFKYI VEKGFICIDG TSLTIIKVDP LSQGGAFYIS MIKHTQDNVI 

       190        200        210        220        230 
MPLKKIGDEV NIEVDLTGKI IEKQILLTLE NQISKKDSTL NTMISNIIEE KVRNYLNK

« Hide

References

« Hide 'large scale' references
[1]"Riboflavin biosynthesis in Saccharomyces cerevisiae. Cloning, characterization, and expression of the RIB5 gene encoding riboflavin synthase."
Santos M.A., Garcia-Ramirez J.J., Revuelta J.L.
J. Biol. Chem. 270:437-444(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"The complete sequence of a 19,482 bp segment located on the right arm of chromosome II from Saccharomyces cerevisiae."
Doignon F., Biteau N., Crouzet M., Aigle M.
Yeast 9:189-199(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[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 SER-95, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z21621 Genomic DNA. Translation: CAA79745.1.
X70529 Genomic DNA. Translation: CAA49920.1.
Z36125 Genomic DNA. Translation: CAA85219.1.
BK006936 Genomic DNA. Translation: DAA07373.1.
PIRS34072.
RefSeqNP_009815.1. NM_001178604.1.

3D structure databases

ProteinModelPortalP38145.
SMRP38145. Positions 1-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32952. 20 interactions.
MINTMINT-4477838.
STRING4932.YBR256C.

Proteomic databases

PaxDbP38145.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR256C; YBR256C; YBR256C.
GeneID852559.
KEGGsce:YBR256C.

Organism-specific databases

CYGDYBR256c.
SGDS000000460. RIB5.

Phylogenomic databases

eggNOGCOG0307.
HOGENOMHOG000151757.
KOK00793.
OMAVVNIERA.
OrthoDBEOG793BMH.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER3O-75.
YEAST:MONOMER3O-75.
UniPathwayUPA00275; UER00405.

Gene expression databases

GenevestigatorP38145.

Family and domain databases

Gene3D2.40.30.20. 2 hits.
InterProIPR023366. ATPase_asu-like.
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. SSF63380. 2 hits.
TIGRFAMsTIGR00187. ribE. 1 hit.
PROSITEPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio971664.
PROP38145.

Entry information

Entry nameRISA_YEAST
AccessionPrimary (citable) accession number: P38145
Secondary accession number(s): D6VQQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 19, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents