Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q43157 (RPE_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:RPE
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
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. Ref.1 Ref.2 Ref.3

Catalytic activity

D-ribulose 5-phosphate = D-xylulose 5-phosphate. Ref.1 Ref.2 Ref.4

Cofactor

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

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Subunit structure

Homooctamer. Ref.2 Ref.4

Subcellular location

Plastidchloroplast thylakoid membrane Ref.3.

Sequence similarities

Belongs to the ribulose-phosphate 3-epimerase family.

Biophysicochemical properties

Kinetic parameters:

KM=250 µM for ribulose 5-phosphate Ref.3 Ref.4

pH dependence:

Optimum pH is 8.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5050Chloroplast Ref.3
Chain51 – 285235Ribulose-phosphate 3-epimerase, chloroplastic
PRO_0000025416

Regions

Region203 – 2064Substrate binding By similarity
Region258 – 2592Substrate binding By similarity

Sites

Active site941Proton acceptor By similarity
Active site2361Proton donor Probable
Metal binding921Divalent metal cation By similarity
Metal binding941Divalent metal cation By similarity
Metal binding1251Divalent metal cation By similarity
Metal binding2361Divalent metal cation By similarity
Binding site671Substrate By similarity
Binding site1251Substrate By similarity
Binding site2381Substrate; via amide nitrogen By similarity

Experimental info

Mutagenesis2361D → A, E or N: Almost abolished enzyme activity. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q43157 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: ED0236FB7B629512

FASTA28530,366
        10         20         30         40         50         60 
MSAASLCQST LQSQINGFCG GLNIRKLQPS TSSPNSLTFT RRKVQTLVKA TSRVDKFSKS 

        70         80         90        100        110        120 
DIIVSPSILS ANFAKLGEQV KAVELAGCDW IHVDVMDGRF VPNITIGPLV VDALRPVTDL 

       130        140        150        160        170        180 
PLDVHLMIVE PEQRVPDFIK AGADIVSVHC ELASTIHLHR TVNQIKSLGA KAGVVLNPGT 

       190        200        210        220        230        240 
PLSTIEYVLD VVDLVLIMSV NPGFGGQSFI ESQVKKISDL RKMCVEKGVN PWIEVDGGVT 

       250        260        270        280 
PANAYKVIEA GANALVAGSA VFGAKDYAEA IKGIKASKRP EPVAV 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42328 mRNA. Translation: AAC41677.1.
AF070941 mRNA. Translation: AAC24708.1.
PIRS62724.

3D structure databases

ProteinModelPortalQ43157.
SMRQ43157. Positions 52-281.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ43157.

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...

Entry information

Entry nameRPE_SPIOL
AccessionPrimary (citable) accession number: Q43157
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 73 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

PATHWAY comments

Index of metabolic and biosynthesis pathways