Summary: RbsD / FucU transport protein family
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RbsD / FucU transport protein family Provide feedback
The Escherichia coli high-affinity ribose-transport system consists of six proteins encoded by the rbs operon (rbsD, rbsA, rbsC, rbsB, rbsK and rbsR). RbsD was originally thought to be a high affinity ribose transport protein, but further analysis [1] shows that it is a D-ribose pyranase . It catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose and beta-allopyranose. This family also includes FucU a component of the fucose operon and is a L-fucose mutarotase, involved in the anomeric conversion of L-fucose. It also exhibits a pyranase activity for D-ribose [1]. Both have been classified in the RbsD/FucU family of proteins. Members of this family are ubiquitous having been found in organisms from eubacteria to mammals.
Literature references
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Feng Y, Jiao W, Fu X, Chang Z;, Protein Sci. 2006;15:1441-1448.: Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein. PUBMED:16731978 EPMC:16731978
External database links
SCOP: | 1oge |
Transporter classification: | 3.A.1 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR007721
RbsD is a component of the ribose operon. It was originally thought to be a high affinity ribose transport protein, but further analysis [ PUBMED:16731978 ] shows that it is a D-ribose pyranase EC . It catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose and beta-allopyranose.
FucU is a component of the fucose operon and is a L-fucose mutarotase EC , involved in the anomeric conversion of L-fucose. It also exhibits a pyranase activity for D-ribose [ PUBMED:16731978 ].
Both have been classified in the RbsD/FucU family of proteins. Members of this family are ubiquitous having been found in organisms from eubacteria to mammals.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | monosaccharide binding (GO:0048029) |
isomerase activity (GO:0016853) | |
Biological process | monosaccharide metabolic process (GO:0005996) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan PELOTA (CL0101), which has the following description:
The members of this clan are all involved in binding to ribose sugar of RNA[1]. Indeed, the key RNA binding residues are conserved across the different families [1]. Members of this clan form mixed alpha-helical and beta-sheet structures [1][2].
The clan contains the following 7 members:
eRF1_3 PELOTA_1 RbsD_FucU Ribosomal_L7Ae RNase_P_pop3 SpoU_sub_bind TSNR_NAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (246) |
Full (3148) |
Representative proteomes | UniProt (16451) |
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RP15 (333) |
RP35 (1429) |
RP55 (3170) |
RP75 (6078) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (246) |
Full (3148) |
Representative proteomes | UniProt (16451) |
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RP15 (333) |
RP35 (1429) |
RP55 (3170) |
RP75 (6078) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_4828 (release 7.6) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Moxon SJ |
Number in seed: | 246 |
Number in full: | 3148 |
Average length of the domain: | 134 aa |
Average identity of full alignment: | 30 % |
Average coverage of the sequence by the domain: | 94.48 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 134 | ||||||||||||
Family (HMM) version: | 16 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
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 RbsD_FucU domain has been found. There are 86 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 sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.