Summary
Domain of unknown function DUF108
This family has no known function. It is found to compose the complete protein in archaebacteria and a single domain in a large C. elegans protein Q19527.
InterPro entry IPR002811
This group contains aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases.
The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(+) cofactor) and a C-terminal alpha/beta domain PUBMED:12496312. This suggested that TM1643 may be a dehydrogenase with the active site located at the interface between the two domains. Enzymatic characterisation of TM1643 revealed that it possesses NAD or NADP-dependent dehydrogenase activity toward l-aspartate but no aspartate oxidase activity PUBMED:12496312. The product of the aspartate dehydrogenase activity is also iminoaspartate. It has been suggested that two different enzymes, an oxidase and a dehydrogenase, may have evolved to catalyse the first step of NAD biosynthesis PUBMED:12496312. Members of this group share some structural similarity to several other NAD(P)+-dependent oxidoreductases, including inositol 1-phosphate synthase, dihydrodipicolinate reductase, and ASA-DH PUBMED:12496312.
It has been proposed that in Thermotoga maritima, TM1643 catalyses the first reaction of de novo biosynthesis of NAD from aspartate, and it produces iminoaspartate required for this pathway. The formation of an enzyme complex between TM1643 and NadA, the next enzyme of the pathway, may allow the channeling of this unstable product directly to the NadA active site PUBMED:12496312.
The same domain is present in animals (e.g., Caenorhabditis elegans F17C8.3 protein).
Gene Ontology
| Molecular function | oxidoreductase activity (GO:0016491) |
| Biological process | pyridine nucleotide biosynthetic process (GO:0019363) |
| NADP catabolic process (GO:0006742) | |
| oxidation reduction (GO:0055114) |
External database links
| PANDIT: | PF01958 |
| SCOP: | 1h2h |
| SYSTERS: | DUF108 |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
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. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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: | none |
| Type: | Family |
| Author: | Enright A, Ouzounis C, Bateman A |
| Number in seed: | 66 |
| Number in full: | 187 |
| Average length of the domain: | 91.50 aa |
| Average identity of full alignment: | 42 % |
| Average coverage of the sequence by the domain: | 34.11 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 92 | ||||||||||||
| Family (HMM) version: | 11 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
There is 1 interaction for this family. More...
NAD_binding_3Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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 DUF108 domain has been found.
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