Reviewed,
UniProtKB/Swiss-Prot Q43157 (RPE_SPIOL)
Last modified
May 5, 2009.
Version 55.
History...
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90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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 |
| ||
| 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)
| Catalytic activity | D-ribulose 5-phosphate = D-xylulose 5-phosphate. Ref.1 Ref.2 |
| Pathway | |
| Subunit structure | Homooctamer. Ref.2 |
| Subcellular location | |
| Sequence similarities | Belongs to the ribulose-phosphate 3-epimerase family. |
| Biophysicochemical properties | Kinetic parameters: KM=250 µM for ribulose 5-phosphate 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 |
| Molecular function | Isomerase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | pentose-phosphate shunt Ref.1 Non-traceable author statement. Source: UniProtKB reductive pentose-phosphate cycle Ref.1Non-traceable author statement. Source: UniProtKB |
| Cellular component | chloroplast thylakoid membrane Ref.3 Inferred from direct assay. Source: UniProtKB |
| Molecular function | ribulose-phosphate 3-epimerase activity Ref.1 Inferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 50 | 50 | Chloroplast Ref.3 | ||||||
| Chain | 51 – 285 | 235 | Ribulose-phosphate 3-epimerase, chloroplastic | PRO_0000025416 | |||||
Sites | |||||||||
| Active site | 236 | 1 | Electrophile Probable | ||||||
Experimental info | |||||||||
| Mutagenesis | 236 | 1 | D → A, E or N: Change in activity. Ref.4 | ||||||
Sequences
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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: 8616224] [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: 9733539] [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: 9523694] [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: 9890975] [Abstract] Cited for: ACTIVE SITE, MUTAGENESIS OF ASP-236. |
Cross-references
Sequence databases | |
|---|---|
| L42328 mRNA. Translation: AAC41677.1. AF070941 mRNA. Translation: AAC24708.1. | |
| PIR | S62724. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1RPX based on UniProtKB Q43843. |
| SMR | Q43157. Positions 52-281. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 5.1.3.1. 286. |
Family and domain databases | |
| InterPro | IPR013785. Aldolase_TIM. IPR000056. Ribul_P_3_epim. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| PANTHER | PTHR11749. Ribul_P_3_epim. 1 hit. |
| Pfam | PF00834. Ribul_P_3_epim. 1 hit. [Graphical view] |
| 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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