Summary: Ribose 5-phosphate isomerase A (phosphoriboisomerase A)
Ribose 5-phosphate isomerase A (phosphoriboisomerase A) Provide feedback
This family consists of several ribose 5-phosphate isomerase A or phosphoriboisomerase A ( EC:188.8.131.52) from bacteria, eukaryotes and archaea.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004788
Ribose 5-phosphate isomerase, also known as phosphoriboisomerase, catalyses the reversible conversion of D-ribose 5-phosphate to D-ribulose 5-phosphate, the first step in the non-oxidative branch of the pentose phosphate pathway [PUBMED:12517338]. This reaction enables ribose to be synthesized from sugars, as well as the recycling of sugars during the degradation of nucleotides. There are two unrelated types of ribose 5-phosphate isomerases: type A (RpiA) is the most common and is found in most organisms, while type B (RpiB) is restricted to specific eukaryotic and prokaryotic species. Escherichia coli produces both RpiA and RpiB (also known as AlsB), although RpiA accounts for 99% of total RPI enzymes [PUBMED:12211039].
This entry represents type A (RpiA) enzymes found in eukaryotes (plants, Metazoa and fungi), bacteria and archaea.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||ribose-5-phosphate isomerase activity (GO:0004751)|
|Biological process||pentose-phosphate shunt, non-oxidative branch (GO:0009052)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
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 superfamily contains a variety of enzymes and non-enzymatic ligand binding domains.
The clan contains the following 11 members:5-FTHF_cyc-lig AcetylCoA_hyd_C AcetylCoA_hydro CitF CoA_trans DeoRC DUF162 Glucosamine_iso IF-2B Rib_5-P_isom_A Sugar-bind
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
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Curation and family details
|Seed source:||Pfam-B_5144 (release 9.0)|
|Number in seed:||58|
|Number in full:||3557|
|Average length of the domain:||171.00 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||74.26 %|
|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:||9|
|Download:||download the raw HMM for this family|
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There are 2 interactions 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 Rib_5-P_isom_A domain has been found. There are 42 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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