Summary: Ribulose-phosphate 3 epimerase family
This is the Wikipedia entry entitled "Ribulose-phosphate 3-epimerase". More...
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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.
Human proteins containing this domain
- Bowien B, Kusian B, Yoo JG, Bednarski R (1992). "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.
- 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.
- 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.
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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)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This large superfamily of TIM barrel enzymes all contain a common phosphate binding site. The phosphate is found in a variety of cofactors and ligands such as FMN [1,2].
The clan contains the following 57 members:Ala_racemase_N ALAD Aldolase AP_endonuc_2 BtpA CdhD CutC DAHP_synth_1 DAHP_synth_2 DeoC DHDPS DHO_dh DHquinase_I DUF1341 DUF2090 DUF556 DUF561 DUF692 DUF993 Dus F_bP_aldolase FMN_dh G3P_antiterm Glu_syn_central Glu_synthase His_biosynth HMGL-like IGPS IMPDH iPGM_N MtrH NanE NAPRTase NeuB NMO OMPdecase Orn_Arg_deC_N Oxidored_FMN PcrB PdxJ PhosphMutase PRAI Pterin_bind QRPTase_C Racemase_4 RhaA Ribul_P_3_epim SOR_SNZ Tagatose_6_P_K ThiG TIM TIM-br_sig_trns TMP-TENI Transaldolase Trp_syntA UvdE UxuA
We make a range of alignments for each Pfam-A family:
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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|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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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