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Q43843

- RPE_SOLTU

UniProt

Q43843 - RPE_SOLTU

Protein

Ribulose-phosphate 3-epimerase, chloroplastic

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    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

    Binds 1 divalent metal cation per subunit. Active with Co2+, Fe2+, Mn2+ and Zn2+ By similarity.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. pentose-phosphate shunt Source: UniProtKB-KW
    2. reductive pentose-phosphate cycle Source: UniProtKB-UniPathway
    3. response to cold Source: EnsemblPlants/Gramene
    4. response to nematode Source: EnsemblPlants/Gramene

    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: 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

    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 – 514
    Beta strandi58 – 625
    Helixi63 – 653
    Helixi68 – 703
    Helixi71 – 8010
    Beta strandi86 – 9712
    Helixi103 – 1097
    Helixi110 – 1123
    Beta strandi117 – 1259
    Helixi126 – 13510
    Beta strandi139 – 1446
    Turni147 – 1493
    Helixi153 – 16210
    Beta strandi165 – 1717
    Helixi177 – 1804
    Turni181 – 1866
    Beta strandi188 – 1958
    Helixi208 – 22215
    Beta strandi227 – 2337
    Turni236 – 2383
    Helixi239 – 2457
    Beta strandi249 – 2535
    Helixi254 – 2574
    Helixi262 – 2709

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    SLGSSTLLQS QISGFGGSQK LQKISFSNPN SLTFTRRRIQ TVVNASSRVD    50
    KFSKSDIIVS PSILSANFSK LGEQVKAIEQ AGCDWIHVDV MDGRFVPNIT 100
    IGPLVVDSLR PITDLPLDVH LMIVEPDQRV PDFIKAGADI VSVHCEQSST 150
    IHLHRTINQI KSLGAKAGVV LNPGTPLTAI EYVLDAVDLV LIMSVNPGFG 200
    GQSFIESQVK KISDLRKICA ERGLNPWIEV DGGVGPKNAY KVIEAGANAL 250
    VAGSAVFGAP DYAEAIKGIK TSKRPEAVAV 280
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50098 mRNA. Translation: CAA90426.1.
    PIRiS68407.
    UniGeneiStu.14340.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50098 mRNA. Translation: CAA90426.1 .
    PIRi S68407.
    UniGenei Stu.14340.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RPX X-ray 2.30 A/B/C 47-276 [» ]
    ProteinModelPortali Q43843.
    SMRi Q43843. Positions 47-276.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q43843.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00116 .

    Miscellaneous databases

    EvolutionaryTracei Q43843.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR000056. Ribul_P_3_epim-like.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view ]
    PANTHERi PTHR11749. PTHR11749. 1 hit.
    Pfami PF00834. Ribul_P_3_epim. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51366. SSF51366. 1 hit.
    TIGRFAMsi TIGR01163. rpe. 1 hit.
    PROSITEi PS01085. RIBUL_P_3_EPIMER_1. 1 hit.
    PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 85 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