Summary: Thiamine-binding protein
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Thiamine-binding protein Provide feedback
The crystal structure of two of these members shows that this domain has a ferredoxin like fold and is likely to exists as at least homodimers. Sulphate ions are are located at the dimer interfaces, which are thought to confer additional stability. Although the function of this domain remains to be identified, its structure suggests a role in protein-protein interactions possibly regulated by the binding of small-molecule ligands [1]. Solution of the structure of the hyperthermophilic anaerobic Thermotoga maritima sequence, UniProtKB:Q9WYV6 shows that this has a beta-alpha-beta-beta-alpha-beta ferredoxin-like fold and assembles as a homotetramer. It was possible to identify a pocket in each monmer that bound an unidentified ligand. It was also found that it bound charged thiamine though not hydroxymethyl pyrimidine. It is proposed that it is transporting charged thiamine around the cytoplasm. Under oxidative conditions this bacterium is under stress, and the transcriiptional unit within which this protein is expressed is up-regulated in these conditions, suggesting that the chelation of cytoplasmic thaimine is part of the response mechanism to such oxidatvie stress, which is mediated by this family [2].
Literature references
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Tao X, Khayat R, Christendat D, Savchenko A, Xu X, Goldsmith-Fischman S, Honig B, Edwards A, Arrowsmith CH, Tong L; , Proteins 2003;52:478-480.: Crystal structures of MTH1187 and its yeast ortholog YBL001c. PUBMED:12866058 EPMC:12866058
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Dermoun Z, Foulon A, Miller MD, Harrington DJ, Deacon AM, Sebban-Kreuzer C, Roche P, Lafitte D, Bornet O, Wilson IA, Dolla A;, J Mol Biol. 2010;400:463-476.: TM0486 from the hyperthermophilic anaerobe Thermotoga maritima is a thiamin-binding protein involved in response of the cell to oxidative conditions. PUBMED:20471400 EPMC:20471400
Internal database links
SCOOP: | Ykof |
Similarity to PfamA using HHSearch: | Ykof |
External database links
SCOP: | 1lxn |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002767
The crystal structure of two of these members shows that this domain has a ferredoxin like fold and is likely to exists as at least homodimers. Sulphate ions are located at the dimer interfaces, which are thought to confer additional stability. Although the function of this domain remains to be identified, its structure suggests a role in protein-protein interactions possibly regulated by the binding of small-molecule ligands [ PUBMED:12866058 ].
Solution of the structure of the hyperthermophilic anaerobic Thermotoga maritima sequence, ( SWISSPROT ), shows that this has a beta-alpha-beta-beta-alpha-beta ferredoxin-like fold and assembles as a homotetramer. It was possible to identify a pocket in each monomer that bound an unidentified ligand. It was also found that it bound charged thiamine though not hydroxymethyl pyrimidine. Under oxidative conditions this bacterium is under stress, and the transcriptional unit within which this protein is expressed is up-regulated in these conditions, suggesting that the chelation of cytoplasmic thaimine is part of the response mechanism to such oxidatvie stress, which is mediated by this family [ PUBMED:20471400 ].
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 MTH1187-YkoF (CL0360), which has the following description:
Putative cell-wall biogenesis proteins and HMP-binding proteins, all with the same Ferredoxin fold, are included in this superfamily.
The clan contains the following 2 members:
Thiamine_BP YkofAlignments
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 (82) |
Full (4009) |
Representative proteomes | UniProt (14169) |
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RP15 (468) |
RP35 (1888) |
RP55 (3952) |
RP75 (6424) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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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 (82) |
Full (4009) |
Representative proteomes | UniProt (14169) |
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RP15 (468) |
RP35 (1888) |
RP55 (3952) |
RP75 (6424) |
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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: | Enright A |
Previous IDs: | DUF77; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Enright A |
Number in seed: | 82 |
Number in full: | 4009 |
Average length of the domain: | 89.8 aa |
Average identity of full alignment: | 30 % |
Average coverage of the sequence by the domain: | 83.2 % |
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: | 92 | ||||||||||||
Family (HMM) version: | 20 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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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 Thiamine_BP domain has been found. There are 27 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.