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Protein

Riboflavin synthase

Gene

RIB5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. oxidoreductase activity Source: InterPro
  2. riboflavin synthase activity Source: SGD

GO - Biological processi

  1. riboflavin biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Riboflavin biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-75.
YEAST:MONOMER3O-75.
UniPathwayiUPA00275; UER00405.

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin synthase (EC:2.5.1.9)
Short name:
RS
Gene namesi
Name:RIB5
Ordered Locus Names:YBR256C
ORF Names:YBR1724
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome II

Organism-specific databases

CYGDiYBR256c.
EuPathDBiFungiDB:YBR256C.
SGDiS000000460. RIB5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Riboflavin synthasePRO_0000068174Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei95 – 951Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38145.
PaxDbiP38145.

Expressioni

Gene expression databases

GenevestigatoriP38145.

Interactioni

Subunit structurei

Homotrimer.By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi32952. 21 interactions.
MINTiMINT-4477838.
STRINGi4932.YBR256C.

Structurei

3D structure databases

ProteinModelPortaliP38145.
SMRiP38145. Positions 1-205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1 – 103103Lumazine-binding 1Add
BLAST
Repeati104 – 205102Lumazine-binding 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni87 – 915Lumazine bindingCurated
Regioni189 – 1935Lumazine bindingCurated

Sequence similaritiesi

Contains 2 lumazine-binding repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0307.
HOGENOMiHOG000151757.
InParanoidiP38145.
KOiK00793.
OMAiMFSGIVA.
OrthoDBiEOG793BMH.

Family and domain databases

Gene3Di2.40.30.20. 2 hits.
InterProiIPR023366. ATPase_asu-like.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR21098. PTHR21098. 1 hit.
PfamiPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFiPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMiSSF63380. SSF63380. 2 hits.
TIGRFAMsiTIGR00187. ribE. 1 hit.
PROSITEiPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38145-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTGIVECMG TVLENNPYDD SESGGQGVSI TIGNAGSILT DCHVGDSIAV
60 70 80 90 100
NGVCLTVTEF NNDSFKVGIS PETIKRSNVA SWIQGTQVNL ERAVSQDVRF
110 120 130 140 150
GGHYVQGHVD TVANIVSRRP EGNSIIFGFQ LRDQEYFKYI VEKGFICIDG
160 170 180 190 200
TSLTIIKVDP LSQGGAFYIS MIKHTQDNVI MPLKKIGDEV NIEVDLTGKI
210 220 230
IEKQILLTLE NQISKKDSTL NTMISNIIEE KVRNYLNK
Length:238
Mass (Da):26,196
Last modified:October 1, 1994 - v1
Checksum:iEA57EAD542D46897
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21621 Genomic DNA. Translation: CAA79745.1.
X70529 Genomic DNA. Translation: CAA49920.1.
Z36125 Genomic DNA. Translation: CAA85219.1.
BK006936 Genomic DNA. Translation: DAA07373.1.
PIRiS34072.
RefSeqiNP_009815.1. NM_001178604.1.

Genome annotation databases

EnsemblFungiiYBR256C; YBR256C; YBR256C.
GeneIDi852559.
KEGGisce:YBR256C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21621 Genomic DNA. Translation: CAA79745.1.
X70529 Genomic DNA. Translation: CAA49920.1.
Z36125 Genomic DNA. Translation: CAA85219.1.
BK006936 Genomic DNA. Translation: DAA07373.1.
PIRiS34072.
RefSeqiNP_009815.1. NM_001178604.1.

3D structure databases

ProteinModelPortaliP38145.
SMRiP38145. Positions 1-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32952. 21 interactions.
MINTiMINT-4477838.
STRINGi4932.YBR256C.

Proteomic databases

MaxQBiP38145.
PaxDbiP38145.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR256C; YBR256C; YBR256C.
GeneIDi852559.
KEGGisce:YBR256C.

Organism-specific databases

CYGDiYBR256c.
EuPathDBiFungiDB:YBR256C.
SGDiS000000460. RIB5.

Phylogenomic databases

eggNOGiCOG0307.
HOGENOMiHOG000151757.
InParanoidiP38145.
KOiK00793.
OMAiMFSGIVA.
OrthoDBiEOG793BMH.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00405.
BioCyciMetaCyc:MONOMER3O-75.
YEAST:MONOMER3O-75.

Miscellaneous databases

NextBioi971664.
PROiP38145.

Gene expression databases

GenevestigatoriP38145.

Family and domain databases

Gene3Di2.40.30.20. 2 hits.
InterProiIPR023366. ATPase_asu-like.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR21098. PTHR21098. 1 hit.
PfamiPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFiPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMiSSF63380. SSF63380. 2 hits.
TIGRFAMsiTIGR00187. ribE. 1 hit.
PROSITEiPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRISA_YEAST
AccessioniPrimary (citable) accession number: P38145
Secondary accession number(s): D6VQQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 29, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.