Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase

Gene

RIB7

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 an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.1 Publication

Catalytic activityi

2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NAD(P)+ = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NAD(P)H.

Pathwayi: riboflavin biosynthesis

This protein is involved in the pathway riboflavin biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway riboflavin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791NADPBy similarity
Binding sitei83 – 831NADPBy similarity
Binding sitei159 – 1591NADP; via amide nitrogen and carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi182 – 1865NADPBy similarity

GO - Molecular functioni

  • 5-amino-6-(5-phosphoribosylamino)uracil reductase activity Source: SGD
  • NADP binding Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Riboflavin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-27.
YEAST:MONOMER3O-27.
UniPathwayiUPA00275.

Names & Taxonomyi

Protein namesi
Recommended name:
2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase (EC:1.1.1.302)
Short name:
DAROPP reductase
Short name:
DARP reductase
Alternative name(s):
2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one reductase
2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase
Short name:
DARIPP synthase
Gene namesi
Name:RIB7
Ordered Locus Names:YBR153W
ORF Names:YBR1203
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR153W.
SGDiS000000357. RIB7.

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene accumulate a 6-hydroxy-2,4,5-triaminopyrimidine derivative.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2442442,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductasePRO_0000135942Add
BLAST

Proteomic databases

MaxQBiP33312.
PeptideAtlasiP33312.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MGM1P322661EBI-15177,EBI-10865

Protein-protein interaction databases

BioGridi32852. 6 interactions.
IntActiP33312. 2 interactions.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 156Combined sources
Helixi19 – 213Combined sources
Beta strandi31 – 388Combined sources
Beta strandi42 – 454Combined sources
Helixi58 – 6710Combined sources
Beta strandi71 – 766Combined sources
Helixi79 – 824Combined sources
Beta strandi101 – 1055Combined sources
Helixi117 – 1237Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi146 – 1494Combined sources
Turni154 – 1563Combined sources
Beta strandi157 – 1593Combined sources
Helixi161 – 17212Combined sources
Beta strandi176 – 1816Combined sources
Helixi183 – 1897Combined sources
Turni193 – 1953Combined sources
Beta strandi197 – 20711Combined sources
Beta strandi223 – 2308Combined sources
Beta strandi232 – 24110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HA7X-ray2.10A/B1-244[»]
4HA9X-ray2.35A/B1-244[»]
ProteinModelPortaliP33312.
SMRiP33312. Positions 8-242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HTP reductase family.Curated

Phylogenomic databases

HOGENOMiHOG000225965.
KOiK14654.
OMAiIAPTWLG.
OrthoDBiEOG7B5X6G.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR024072. DHFR-like_dom.
IPR011549. RibD_C.
IPR002734. RibDG_C.
[Graphical view]
PfamiPF01872. RibD_C. 1 hit.
[Graphical view]
SUPFAMiSSF53597. SSF53597. 1 hit.
TIGRFAMsiTIGR00227. ribD_Cterm. 1 hit.

Sequencei

Sequence statusi: Complete.

P33312-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLTPLCEDL PQFLQNYLPN AGQTENTIVP FVTLTYAQSL DARVSRGPGV
60 70 80 90 100
RTTISHPETK TMTHYLRHHH DGILVGSGTV LADNPGLNCK WGPDPAANSP
110 120 130 140 150
RPIIIDTKQK WRFDGSKMQE LFIKRQGKPP IVVVTSEPII KEQHVDYAIC
160 170 180 190 200
PINDTTKLVD WKKLFEILKE EFNIRSVMVE GGANVINQLL LRSDIVNSLI
210 220 230 240
ITIGSTFLGS SGTEVSPPQT VNLKDMSWWK GITDVVLCAR LADD
Length:244
Mass (Da):27,116
Last modified:February 1, 1994 - v1
Checksum:iBB19A9D2A1A8D7DB
GO

Sequence cautioni

The sequence AAC60554.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21622 Genomic DNA. Translation: CAA79746.1.
X71329 Genomic DNA. Translation: CAA50471.1.
S59774 Genomic DNA. Translation: AAC60554.1. Different initiation.
Z36022 Genomic DNA. Translation: CAA85112.1.
AY557713 Genomic DNA. Translation: AAS56039.1.
BK006936 Genomic DNA. Translation: DAA07268.1.
PIRiS40698.
RefSeqiNP_009711.3. NM_001178501.3.

Genome annotation databases

EnsemblFungiiYBR153W; YBR153W; YBR153W.
GeneIDi852450.
KEGGisce:YBR153W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21622 Genomic DNA. Translation: CAA79746.1.
X71329 Genomic DNA. Translation: CAA50471.1.
S59774 Genomic DNA. Translation: AAC60554.1. Different initiation.
Z36022 Genomic DNA. Translation: CAA85112.1.
AY557713 Genomic DNA. Translation: AAS56039.1.
BK006936 Genomic DNA. Translation: DAA07268.1.
PIRiS40698.
RefSeqiNP_009711.3. NM_001178501.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HA7X-ray2.10A/B1-244[»]
4HA9X-ray2.35A/B1-244[»]
ProteinModelPortaliP33312.
SMRiP33312. Positions 8-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32852. 6 interactions.
IntActiP33312. 2 interactions.

Proteomic databases

MaxQBiP33312.
PeptideAtlasiP33312.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR153W; YBR153W; YBR153W.
GeneIDi852450.
KEGGisce:YBR153W.

Organism-specific databases

EuPathDBiFungiDB:YBR153W.
SGDiS000000357. RIB7.

Phylogenomic databases

HOGENOMiHOG000225965.
KOiK14654.
OMAiIAPTWLG.
OrthoDBiEOG7B5X6G.

Enzyme and pathway databases

UniPathwayiUPA00275.
BioCyciMetaCyc:MONOMER3O-27.
YEAST:MONOMER3O-27.

Miscellaneous databases

PROiP33312.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR024072. DHFR-like_dom.
IPR011549. RibD_C.
IPR002734. RibDG_C.
[Graphical view]
PfamiPF01872. RibD_C. 1 hit.
[Graphical view]
SUPFAMiSSF53597. SSF53597. 1 hit.
TIGRFAMsiTIGR00227. ribD_Cterm. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the RIB7 gene from Saccharomyces cerevisiae."
    Buitrago M.J., Garcia-Ramirez J.J., Revuelta J.L.
    Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence of a 4.8 kb fragment of Saccharomyces cerevisiae chromosome II including three essential open reading frames."
    Baur A., Schaaff-Gerstenschlaeger I., Boles E., Miosga T., Rose M., Zimmermann F.K.
    Yeast 9:289-293(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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Biosynthesis of riboflavine in Saccharomyces cerevisiae: the role of genes rib 1 and rib 7."
    Oltmanns O., Bacher A.
    J. Bacteriol. 110:818-822(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: ATCC 204508 / S288c.

Entry informationi

Entry nameiRIB7_YEAST
AccessioniPrimary (citable) accession number: P33312
Secondary accession number(s): D6VQE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 8, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.