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Protein

Ribose-5-phosphate isomerase

Gene

RKI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-ribose 5-phosphate = D-ribulose 5-phosphate.

Pathwayi: pentose phosphate pathway

This protein is involved in step 1 of the subpathway that synthesizes D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage).
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-5-phosphate isomerase (RKI1)
This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • ribose-5-phosphate isomerase activity Source: SGD

GO - Biological processi

  • pentose-phosphate shunt Source: SGD
  • pentose-phosphate shunt, non-oxidative branch Source: InterPro
  • pyridoxine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciYEAST:YOR095C-MONOMER.
ReactomeiR-SCE-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKQ12189.
UniPathwayiUPA00115; UER00412.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-5-phosphate isomerase (EC:5.3.1.6)
Alternative name(s):
D-ribose-5-phosphate ketol-isomerase
Phosphoriboisomerase
Gene namesi
Name:RKI1
Ordered Locus Names:YOR095C
ORF Names:YOR3174C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR095C.
SGDiS000005621. RKI1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Ribose-5-phosphate isomerasePRO_0000158524Add
BLAST

Proteomic databases

MaxQBiQ12189.
PeptideAtlasiQ12189.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-15898,EBI-15898

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi34493. 28 interactions.
DIPiDIP-4155N.
IntActiQ12189. 8 interactions.
MINTiMINT-544335.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 3314Combined sources
Turni36 – 383Combined sources
Beta strandi41 – 444Combined sources
Helixi51 – 6111Combined sources
Turni64 – 663Combined sources
Helixi67 – 704Combined sources
Beta strandi74 – 796Combined sources
Helixi80 – 889Combined sources
Turni96 – 983Combined sources
Beta strandi101 – 1077Combined sources
Beta strandi110 – 1123Combined sources
Helixi126 – 1338Combined sources
Beta strandi136 – 1449Combined sources
Helixi145 – 1473Combined sources
Beta strandi150 – 1534Combined sources
Beta strandi161 – 1655Combined sources
Helixi167 – 1693Combined sources
Helixi170 – 17910Combined sources
Beta strandi184 – 1885Combined sources
Turni192 – 1943Combined sources
Beta strandi195 – 1984Combined sources
Beta strandi206 – 2116Combined sources
Beta strandi213 – 2164Combined sources
Helixi218 – 2269Combined sources
Beta strandi231 – 2377Combined sources
Beta strandi242 – 2476Combined sources
Beta strandi253 – 2586Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XTZX-ray2.10A1-258[»]
ProteinModelPortaliQ12189.
SMRiQ12189. Positions 19-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12189.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000004352.
HOGENOMiHOG000276369.
InParanoidiQ12189.
KOiK01807.
OMAiFIFDAFW.
OrthoDBiEOG7JMGRX.

Family and domain databases

InterProiIPR004788. Ribose5P_isomerase_typA.
[Graphical view]
PANTHERiPTHR11934. PTHR11934. 1 hit.
PfamiPF06026. Rib_5-P_isom_A. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00021. rpiA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q12189-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGVPKIDA LESLGNPLED AKRAAAYRAV DENLKFDDHK IIGIGSGSTV
60 70 80 90 100
VYVAERIGQY LHDPKFYEVA SKFICIPTGF QSRNLILDNK LQLGSIEQYP
110 120 130 140 150
RIDIAFDGAD EVDENLQLIK GGGACLFQEK LVSTSAKTFI VVADSRKKSP
160 170 180 190 200
KHLGKNWRQG VPIEIVPSSY VRVKNDLLEQ LHAEKVDIRQ GGSAKAGPVV
210 220 230 240 250
TDNNNFIIDA DFGEISDPRK LHREIKLLVG VVETGLFIDN ASKAYFGNSD

GSVEVTEK
Length:258
Mass (Da):28,258
Last modified:November 1, 1996 - v1
Checksum:iE9F72BF2759F4DDD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94335 Genomic DNA. Translation: CAA64017.1.
Z75003 Genomic DNA. Translation: CAA99292.1.
BK006948 Genomic DNA. Translation: DAA10872.1.
PIRiS61656.
RefSeqiNP_014738.1. NM_001183514.1.

Genome annotation databases

EnsemblFungiiYOR095C; YOR095C; YOR095C.
GeneIDi854262.
KEGGisce:YOR095C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94335 Genomic DNA. Translation: CAA64017.1.
Z75003 Genomic DNA. Translation: CAA99292.1.
BK006948 Genomic DNA. Translation: DAA10872.1.
PIRiS61656.
RefSeqiNP_014738.1. NM_001183514.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XTZX-ray2.10A1-258[»]
ProteinModelPortaliQ12189.
SMRiQ12189. Positions 19-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34493. 28 interactions.
DIPiDIP-4155N.
IntActiQ12189. 8 interactions.
MINTiMINT-544335.

Proteomic databases

MaxQBiQ12189.
PeptideAtlasiQ12189.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR095C; YOR095C; YOR095C.
GeneIDi854262.
KEGGisce:YOR095C.

Organism-specific databases

EuPathDBiFungiDB:YOR095C.
SGDiS000005621. RKI1.

Phylogenomic databases

GeneTreeiENSGT00390000004352.
HOGENOMiHOG000276369.
InParanoidiQ12189.
KOiK01807.
OMAiFIFDAFW.
OrthoDBiEOG7JMGRX.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00412.
BioCyciYEAST:YOR095C-MONOMER.
ReactomeiR-SCE-71336. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKQ12189.

Miscellaneous databases

EvolutionaryTraceiQ12189.
PROiQ12189.

Family and domain databases

InterProiIPR004788. Ribose5P_isomerase_typA.
[Graphical view]
PANTHERiPTHR11934. PTHR11934. 1 hit.
PfamiPF06026. Rib_5-P_isom_A. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00021. rpiA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Cloning and characterization of the first two genes of the non-oxidative part of the Saccharomyces cerevisiae pentose-phosphate pathway."
    Miosga T., Zimmermann F.K.
    Curr. Genet. 30:404-409(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRPIA_YEAST
AccessioniPrimary (citable) accession number: Q12189
Secondary accession number(s): D6W2F6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 141 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 5680 molecules/cell in log phase SD medium.1 Publication

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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.