Summary: D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase
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D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase Provide feedback
Bacterial enzyme splits fructose-6-P and/or xylulose-5-P with the aid of inorganic phosphate into either acetyl-P and erythrose-4-P and/or acetyl-P and glyeraldehyde-3-P EC:188.8.131.52, EC:184.108.40.206 . This family is distantly related to transketolases e.g. PF02779.
Meile L, Rohr LM, Geissmann TA, Herensperger M, Teuber M; , J Bacteriol 2001;183:2929-2936.: Characterization of the D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase gene (xfp) from Bifidobacterium lactis. PUBMED:11292814 EPMC:11292814
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005593
Phosphoketolases (PK) are key enzymes of the pentose phosphate pathway of heterofermentative and facultative homofermentative lactic acid bacteria and of the D-fructose 6-phosphate shunt of bifidobacteria. PK activity has been sporadically reported in other microorganisms including eukaryotic yeasts. Xylulose-5-phosphate/fructose-6-phosphate phosphoketolase is a thiamine diphosphate (ThdP)-dependent enzyme found in bacteria such as Bifidobacterium sp [PUBMED:11292814, PUBMED:15899413]. This enzyme has dual-specificity with the following catalytic activities:
Phosphoketolases are distantly related to transketolases, e.g. INTERPRO.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||aldehyde-lyase activity (GO:0016832)|
|Biological process||carbohydrate metabolic process (GO:0005975)|
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This clan includes pyruvate dehydrogenases, branched chain alpha-keto acid decarboxylases, phosphoketolases and the pyrimidine binding region of transketolases.
The clan contains the following 9 members:DXP_synthase_N E1_dh POR_N TPP_enzyme_C TPP_enzyme_N Transket_pyr Transketolase_N XFP XFP_N
We make a range of alignments for each Pfam-A family:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Curation and family details
|Seed source:||Wood V|
|Author:||Wood V, Bateman A|
|Number in seed:||6|
|Number in full:||1182|
|Average length of the domain:||168.90 aa|
|Average identity of full alignment:||47 %|
|Average coverage of the sequence by the domain:||22.78 %|
|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:||10|
|Download:||download the raw HMM for this family|
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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 XFP domain has been found. There are 16 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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