Ribulose-phosphate 3-epimerase, chloroplastic precursor

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Q43157 (RPE_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

RPE

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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⁺, Mn²⁺ and Zn²⁺ By similarity.
Pathway	Carbohydrate biosynthesis; Calvin cycle.
Subunit structure	Homooctamer. Ref.2 Ref.4
Subcellular location	Plastid › chloroplast thylakoid membrane Ref.3.
Sequence similarities	Belongs to the ribulose-phosphate 3-epimerase family.
Biophysicochemical properties	Kinetic parameters: K_M=250 µM for ribulose 5-phosphate Ref.3 Ref.4 pH dependence: Optimum pH is 8.5.

Ontologies

Keywords
Biological process	Calvin cycle Carbohydrate metabolism Pentose shunt
Cellular component	Chloroplast Membrane Plastid Thylakoid
Domain	Transit peptide
Ligand	Cobalt Manganese Metal-binding Zinc
Molecular function	Isomerase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	pentose-phosphate shunt Non-traceable author statement Ref.1. Source: UniProtKB reductive pentose-phosphate cycle Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	chloroplast thylakoid membrane Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribulose-phosphate 3-epimerase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 50

Chloroplast Ref.3

Chain

51 – 285

235

Ribulose-phosphate 3-epimerase, chloroplastic

PRO_0000025416

Regions

Region

203 – 206

Substrate binding By similarity

Region

258 – 259

Substrate binding By similarity

Sites

Active site

Proton acceptor By similarity

Active site

236

Proton donor Probable

Metal binding

Divalent metal cation By similarity

Metal binding

Divalent metal cation By similarity

Metal binding

125

Divalent metal cation By similarity

Metal binding

236

Divalent metal cation By similarity

Binding site

Substrate By similarity

Binding site

125

Substrate By similarity

Binding site

238

Substrate; via amide nitrogen By similarity

Experimental info

Mutagenesis

236

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

Sequences

Sequence

Length

Mass (Da)

Tools

Q43157 [UniParc].

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

285

30,366

        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.
PIR	S62724.
3D structure databases
ProteinModelPortal	Q43157.
SMR	Q43157. Positions 52-281.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00116.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR000056. Ribul_P_3_epim-like. IPR011060. RibuloseP-bd_barrel. [Graphical view]
PANTHER	PTHR11749. PTHR11749. 1 hit.
Pfam	PF00834. Ribul_P_3_epim. 1 hit. [Graphical view]
SUPFAM	SSF51366. RibP_bind_barrel. 1 hit.
TIGRFAMs	TIGR01163. rpe. 1 hit.
PROSITE	PS01085. RIBUL_P_3_EPIMER_1. 1 hit. PS01086. RIBUL_P_3_EPIMER_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RPE_SPIOL

Accession

Primary (citable) accession number: Q43157

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents