Summary: Ribulose-phosphate 3 epimerase family
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Ribulose-phosphate 3-epimerase Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
|Ribulose-phosphate 3 epimerase family|
In enzymology, a ribulose-phosphate 3-epimerase (EC 18.104.22.168) (also known as pentose-5-phosphate 3-epimerase or PPE) is the enzyme that converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle.
- D-ribulose 5-phosphate D-xylulose 5-phosphate
In Alcaligenes eutrophus two copies of the gene coding for PPE are known, one is chromosomally encoded , the other one is on a plasmid . PPE has been found in a wide range of bacteria, archaebacteria, fungi and plants. All the proteins have from 209 to 241 amino acid residues. The enzyme has a TIM barrel structure.
The systematic name of this enzyme class is D-ribulose-5-phosphate 3-epimerase. Other names in common use include phosphoribulose epimerase, erythrose-4-phosphate isomerase, phosphoketopentose 3-epimerase, xylulose phosphate 3-epimerase, phosphoketopentose epimerase, ribulose 5-phosphate 3-epimerase, D-ribulose phosphate-3-epimerase, D-ribulose 5-phosphate epimerase, D-ribulose-5-P 3-epimerase, D-xylulose-5-phosphate 3-epimerase, and pentose-5-phosphate 3-epimerase.
 Structural studies
 Human proteins containing this domain
- Bowien B, Kusian B, Yoo JG, Bednarski R (1992). [//www.ncbi.nlm.nih.gov/pmc/articles/PMC207429/ "The Calvin cycle enzyme pentose-5-phosphate 3-epimeras e is encoded within the cfx operons of the chemoautotroph Alcaligenes eutrophus"]. J. Bacteriol. 174 (22): 7337–7344. PMC 207429. PMID 1429456. //www.ncbi.nlm.nih.gov/pmc/articles/PMC207429/.
- Ashwell G and Hickman J (1957). "Enzymatic formation of xylulose 5-phosphate from ribose 5-phosphate in spleen". J. Biol. Chem. 226 (1): 65–76. PMID 13428737.
- DICKENS F, WILLIAMSON DH (1956). "Pentose phosphate isomerase and epimerase from animal tissues". Biochem. J. 64 (3): 567–78. PMC 1199776. PMID 13373810. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1199776/.
- Hurwitz J and Horecker BL (1956). "The purification of phosphoketopentoepimerase from Lactobacillus pentosus and the preparation of xylulose 5-phosphate". J. Biol. Chem. 223 (2): 993–1008. PMID 13385247.
- Stumpf PK and Horecker BL (1956). "The roole of xylulose 5-phosphate in xylose metabolism of Lactobacillus pentosus". J. Biol. Chem. 218: 753–768.
- Terada T, Mukae H, Ohashi K, Hosomi S, Mizoguchi T, Uehara K (1985). "Characterization of an enzyme which catalyzes isomerization and epimerization of D-erythrose 4-phosphate". Eur. J. Biochem. 148 (2): 345–51. doi:10.1111/j.1432-1033.1985.tb08845.x. PMID 3987693.
|This isomerase article is a stub. You can help Wikipedia by expanding it.|
Ribulose-phosphate 3 epimerase family Provide feedback
This enzyme catalyses the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.
Internal database links
|Similarity to PfamA using HHSearch:||QRPTase_C|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000056Ribulose-phosphate 3-epimerase (EC) (also known as pentose-5-phosphate 3-epimerase or PPE) is the enzyme that converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. In Ralstonia eutropha (Alcaligenes eutrophus) two copies of the gene coding for PPE are known [PUBMED:1429456], one is chromosomally encoded SWISSPROT, the other one is on a plasmid SWISSPROT. PPE has been found in a wide range of bacteria, archaebacteria, fungi and plants. All the proteins have from 209 to 241 amino acid residues. The enzyme has a TIM barrel structure. This family also includes other enzymes from the ribulose-phosphate 3-epimerase family, like D-allulose-6-phosphate 3-epimerase and other putative pentose-5-phosphate 3-epimerases. D-allulose-6-phosphate 3-epimerase catalyses the reversible epimerization of D-allulose 6-phosphate to D-fructose 6-phosphate, but it can also catalyse with lower efficiency the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate [PUBMED:18700786].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||racemase and epimerase activity, acting on carbohydrates and derivatives (GO:0016857)|
|Biological process||carbohydrate metabolic process (GO:0005975)|
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Curation and family details
|Seed source:||Pfam-B_1291 (release 2.1)|
|Number in seed:||13|
|Number in full:||6022|
|Average length of the domain:||198.40 aa|
|Average identity of full alignment:||43 %|
|Average coverage of the sequence by the domain:||88.92 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Ribul_P_3_epim domain has been found. There are 50 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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