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Q43843 (RPE_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length280 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 divalent metal cation per subunit. Active with Co2+, Fe2+, Mn2+ and Zn2+ By similarity.

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Subunit structure

Homohexamer. Ref.2

Subcellular location

Plastidchloroplast thylakoid membrane.

Tissue specificity

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

Sequence similarities

Belongs to the ribulose-phosphate 3-epimerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – 45›45Chloroplast
Chain46 – 280235Ribulose-phosphate 3-epimerase, chloroplastic
PRO_0000025417

Regions

Region198 – 2014Substrate binding By similarity
Region253 – 2542Substrate binding By similarity

Sites

Active site891Proton acceptor By similarity
Active site2311Proton donor By similarity
Metal binding871Divalent metal cation By similarity
Metal binding891Divalent metal cation By similarity
Metal binding1201Divalent metal cation By similarity
Metal binding2311Divalent metal cation By similarity
Binding site621Substrate By similarity
Binding site1201Substrate By similarity
Binding site2331Substrate; via amide nitrogen By similarity

Experimental info

Non-terminal residue11

Secondary structure

.......................................... 280
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q43843 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 3381A798F056491C

FASTA28029,881
        10         20         30         40         50         60 
SLGSSTLLQS QISGFGGSQK LQKISFSNPN SLTFTRRRIQ TVVNASSRVD KFSKSDIIVS 

        70         80         90        100        110        120 
PSILSANFSK LGEQVKAIEQ AGCDWIHVDV MDGRFVPNIT IGPLVVDSLR PITDLPLDVH 

       130        140        150        160        170        180 
LMIVEPDQRV PDFIKAGADI VSVHCEQSST IHLHRTINQI KSLGAKAGVV LNPGTPLTAI 

       190        200        210        220        230        240 
EYVLDAVDLV LIMSVNPGFG GQSFIESQVK KISDLRKICA ERGLNPWIEV DGGVGPKNAY 

       250        260        270        280 
KVIEAGANAL VAGSAVFGAP DYAEAIKGIK TSKRPEAVAV 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z50098 mRNA. Translation: CAA90426.1.
PIRS68407.
UniGeneStu.14340.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RPXX-ray2.30A/B/C47-276[»]
ProteinModelPortalQ43843.
SMRQ43843. Positions 47-276.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ43843.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00116.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERPTHR11749. PTHR11749. 1 hit.
PfamPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR01163. rpe. 1 hit.
PROSITEPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ43843.

Entry information

Entry nameRPE_SOLTU
AccessionPrimary (citable) accession number: Q43843
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways