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Protein

Ribulose-phosphate 3-epimerase, chloroplastic

Gene

RPE

Organism
Spinacia oleracea (Spinach)
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.3 Publications

Catalytic activityi

D-ribulose 5-phosphate = D-xylulose 5-phosphate.3 Publications

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

Kineticsi

  1. KM=250 µM for ribulose 5-phosphate2 Publications

    pH dependencei

    Optimum pH is 8.5.2 Publications

    Pathway:iCalvin cycle

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei67 – 671SubstrateBy similarity
    Metal bindingi92 – 921Divalent metal cationBy similarity
    Active sitei94 – 941Proton acceptorBy similarity
    Metal bindingi94 – 941Divalent metal cationBy similarity
    Metal bindingi125 – 1251Divalent metal cationBy similarity
    Binding sitei125 – 1251SubstrateBy similarity
    Active sitei236 – 2361Proton donor1 Publication
    Metal bindingi236 – 2361Divalent metal cationBy similarity
    Binding sitei238 – 2381Substrate; via amide nitrogenBy similarity

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • ribulose-phosphate 3-epimerase activity Source: UniProtKB

    GO - Biological processi

    • pentose-phosphate shunt Source: UniProtKB
    • reductive pentose-phosphate cycle Source: UniProtKB
    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

    BRENDAi5.1.3.1. 5812.
    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
    Gene namesi
    Name:RPE
    OrganismiSpinacia oleracea (Spinach)
    Taxonomic identifieri3562 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast thylakoid membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Membrane, Plastid, Thylakoid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi236 – 2361D → A, E or N: Almost abolished enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5050Chloroplast1 PublicationAdd
    BLAST
    Chaini51 – 285235Ribulose-phosphate 3-epimerase, chloroplasticPRO_0000025416Add
    BLAST

    Proteomic databases

    PRIDEiQ43157.

    Interactioni

    Subunit structurei

    Homooctamer.2 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliQ43157.
    SMRiQ43157. Positions 52-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni203 – 2064Substrate bindingBy similarity
    Regioni258 – 2592Substrate 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: Complete.

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

    Q43157-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSAASLCQST LQSQINGFCG GLNIRKLQPS TSSPNSLTFT RRKVQTLVKA
    60 70 80 90 100
    TSRVDKFSKS DIIVSPSILS ANFAKLGEQV KAVELAGCDW IHVDVMDGRF
    110 120 130 140 150
    VPNITIGPLV VDALRPVTDL PLDVHLMIVE PEQRVPDFIK AGADIVSVHC
    160 170 180 190 200
    ELASTIHLHR TVNQIKSLGA KAGVVLNPGT PLSTIEYVLD VVDLVLIMSV
    210 220 230 240 250
    NPGFGGQSFI ESQVKKISDL RKMCVEKGVN PWIEVDGGVT PANAYKVIEA
    260 270 280
    GANALVAGSA VFGAKDYAEA IKGIKASKRP EPVAV
    Length:285
    Mass (Da):30,366
    Last modified:November 1, 1996 - v1
    Checksum:iED0236FB7B629512
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L42328 mRNA. Translation: AAC41677.1.
    AF070941 mRNA. Translation: AAC24708.1.
    PIRiS62724.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L42328 mRNA. Translation: AAC41677.1.
    AF070941 mRNA. Translation: AAC24708.1.
    PIRiS62724.

    3D structure databases

    ProteinModelPortaliQ43157.
    SMRiQ43157. Positions 52-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiQ43157.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00116.
    BRENDAi5.1.3.1. 5812.

    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. "Cloning of the amphibolic Calvin cycle/OPPP enzyme D-ribulose-5-phosphate 3-epimerase (EC 5.1.3.1) from spinach chloroplasts: functional and evolutionary aspects."
      Nowitzki U., Wyrich R., Westhoff P., Henze K., Schnarrenberger C., Martin W.F.
      Plant Mol. Biol. 29:1279-1291(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
    2. "D-ribulose-5-phosphate 3-epimerase: cloning and heterologous expression of the spinach gene, and purification and characterization of the recombinant enzyme."
      Chen Y.-R., Hartman F.C., Lu T.-Y.S., Larimer F.W.
      Plant Physiol. 118:199-207(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
      Strain: cv. Melody.
    3. "Purification, properties and in situ localization of the amphibolic enzymes D-ribulose 5-phosphate 3-epimerase and transketolase from spinach chloroplasts."
      Teige M., Melzer M., Suess K.-H.
      Eur. J. Biochem. 252:237-244(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 51-66, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
      Strain: cv. Matador.
    4. "Identification of a catalytic aspartyl residue of D-ribulose 5-phosphate 3-epimerase by site-directed mutagenesis."
      Chen Y.-R., Larimer F.W., Serpersu E.H., Hartman F.C.
      J. Biol. Chem. 274:2132-2136(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ASP-236.

    Entry informationi

    Entry nameiRPE_SPIOL
    AccessioniPrimary (citable) accession number: Q43157
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: April 1, 2015
    This is version 76 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

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. 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.