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Protein

Ribulose-phosphate 3-epimerase, chloroplastic

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.

Catalytic activityi

D-ribulose 5-phosphate = D-xylulose 5-phosphate.

Cofactori

Co2+By similarity, Fe2+By similarity, Mn2+By similarity, Zn2+By similarityNote: Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn2+.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621SubstrateBy similarity
Metal bindingi87 – 871Divalent metal cationBy similarity
Active sitei89 – 891Proton acceptorBy similarity
Metal bindingi89 – 891Divalent metal cationBy similarity
Metal bindingi120 – 1201Divalent metal cationBy similarity
Binding sitei120 – 1201SubstrateBy similarity
Active sitei231 – 2311Proton donorBy similarity
Metal bindingi231 – 2311Divalent metal cationBy similarity
Binding sitei233 – 2331Substrate; via amide nitrogenBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. ribulose-phosphate 3-epimerase activity Source: UniProtKB

GO - Biological processi

  1. defense response to bacterium Source: EnsemblPlants/Gramene
  2. pentose-phosphate shunt Source: UniProtKB-KW
  3. reductive pentose-phosphate cycle Source: UniProtKB-UniPathway
  4. response to nematode Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Calvin cycle, Carbohydrate metabolism, Pentose shunt

Keywords - Ligandi

Cobalt, Iron, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose-phosphate 3-epimerase, chloroplastic (EC:5.1.3.1)
Alternative name(s):
Pentose-5-phosphate 3-epimerase
Short name:
PPE
R5P3E
Short name:
RPE
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: EnsemblPlants/Gramene
  2. chloroplast envelope Source: EnsemblPlants/Gramene
  3. chloroplast stroma Source: EnsemblPlants/Gramene
  4. chloroplast thylakoid membrane Source: UniProtKB
  5. stromule Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei‹1 – 45›45ChloroplastAdd
BLAST
Chaini46 – 280235Ribulose-phosphate 3-epimerase, chloroplasticPRO_0000025417Add
BLAST

Proteomic databases

PRIDEiQ43843.

Expressioni

Tissue specificityi

Highest level of expression in leaves, whereas it is low in roots, tubers, and stems.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Structurei

Secondary structure

1
280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 514Combined sources
Beta strandi58 – 625Combined sources
Helixi63 – 653Combined sources
Helixi68 – 703Combined sources
Helixi71 – 8010Combined sources
Beta strandi86 – 9712Combined sources
Helixi103 – 1097Combined sources
Helixi110 – 1123Combined sources
Beta strandi117 – 1259Combined sources
Helixi126 – 13510Combined sources
Beta strandi139 – 1446Combined sources
Turni147 – 1493Combined sources
Helixi153 – 16210Combined sources
Beta strandi165 – 1717Combined sources
Helixi177 – 1804Combined sources
Turni181 – 1866Combined sources
Beta strandi188 – 1958Combined sources
Helixi208 – 22215Combined sources
Beta strandi227 – 2337Combined sources
Turni236 – 2383Combined sources
Helixi239 – 2457Combined sources
Beta strandi249 – 2535Combined sources
Helixi254 – 2574Combined sources
Helixi262 – 2709Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RPXX-ray2.30A/B/C47-276[»]
ProteinModelPortaliQ43843.
SMRiQ43843. Positions 47-276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ43843.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 2014Substrate bindingBy similarity
Regioni253 – 2542Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01163. rpe. 1 hit.
PROSITEiPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q43843-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SLGSSTLLQS QISGFGGSQK LQKISFSNPN SLTFTRRRIQ TVVNASSRVD
60 70 80 90 100
KFSKSDIIVS PSILSANFSK LGEQVKAIEQ AGCDWIHVDV MDGRFVPNIT
110 120 130 140 150
IGPLVVDSLR PITDLPLDVH LMIVEPDQRV PDFIKAGADI VSVHCEQSST
160 170 180 190 200
IHLHRTINQI KSLGAKAGVV LNPGTPLTAI EYVLDAVDLV LIMSVNPGFG
210 220 230 240 250
GQSFIESQVK KISDLRKICA ERGLNPWIEV DGGVGPKNAY KVIEAGANAL
260 270 280
VAGSAVFGAP DYAEAIKGIK TSKRPEAVAV
Length:280
Mass (Da):29,881
Last modified:November 1, 1997 - v1
Checksum:i3381A798F056491C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50098 mRNA. Translation: CAA90426.1.
PIRiS68407.
UniGeneiStu.14340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50098 mRNA. Translation: CAA90426.1.
PIRiS68407.
UniGeneiStu.14340.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RPXX-ray2.30A/B/C47-276[»]
ProteinModelPortaliQ43843.
SMRiQ43843. Positions 47-276.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ43843.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00116.

Miscellaneous databases

EvolutionaryTraceiQ43843.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01163. rpe. 1 hit.
PROSITEiPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Chloroplast pentose-5-phosphate 3-epimerase from potato: cloning, cDNA sequence, and tissue-specific enzyme accumulation."
    Teige M., Kopriva S., Bauwe H., Suess K.-H.
    FEBS Lett. 377:349-352(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Desiree.
    Tissue: Leaf.
  2. "Structure and mechanism of the amphibolic enzyme D-ribulose-5-phosphate 3-epimerase from potato chloroplasts."
    Kopp J., Kopriva S., Suess K.-H., Schulz G.E.
    J. Mol. Biol. 287:761-771(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiRPE_SOLTU
AccessioniPrimary (citable) accession number: Q43843
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

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.