Summary: C-terminal regulatory domain of Threonine dehydratase
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C-terminal regulatory domain of Threonine dehydratase Provide feedback
Threonine dehydratases PF00291 all contain a carboxy terminal region. This region may have a regulatory role. Some members contain two copies of this region. This family is homologous to the PF01842 domain.
Literature references
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Gallagher DT, Gilliland GL, Xiao G, Zondlo J, Fisher KE, Chinchilla D, Eisenstein E; , Structure 1998;6:465-475.: Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase. PUBMED:9562556 EPMC:9562556
External database links
HOMSTRAD: | Thr_dehydrat_C |
SCOP: | 1tdj |
This tab holds annotation information from the InterPro database.
InterPro entry IPR001721
Threonine deaminase (threonine dehydratase, TD) is the first enzyme on the pathway for the biosynthesis of isoleucine. TD is organized into two domains. The larger N-terminal domain is considered the catalytic domain as it contains the essential pyridoxal phosphate cofactor. The C-terminal regulatory domain folds as an eight-stranded antiparallel sheet. The holoenzyme is a homotetramer in which the intersubunit contacts lie between pairs of C-terminal regulatory domains and pairs of N-terminal domains [ PUBMED:9562556 ].
The ACT domain is a 90 amino acid long domain, which has been named after three of the allosterically regulated enzymes in which it is found: aspartate kinase, chorismate mutase and TyrA (prephenate dehydrogenase) [ PUBMED:10222208 ]. The ACT domain is found in a variety of contexts and is proposed to be a structurally conserved regulatory domain involved in the binding of small ligands, such as amino acids. There is a close structural and functional relationship between the regulatory domain of TD and the ACT domain [ PUBMED:11751050 ].
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 ACT (CL0070), which has the following description:
These domains are involved in binding to amino-acids and causing allosteric regulation of linked enzyme domains [1]. The relationship between these two families was first noticed in [2].
The clan contains the following 12 members:
ACT ACT_3 ACT_4 ACT_5 ACT_6 ACT_7 ACT_8 ALS_ss_C DUF493 NikR_C NIL Thr_dehydrat_CAlignments
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 (12) |
Full (7645) |
Representative proteomes | UniProt (33007) |
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RP15 (999) |
RP35 (3468) |
RP55 (7265) |
RP75 (13062) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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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 (12) |
Full (7645) |
Representative proteomes | UniProt (33007) |
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RP15 (999) |
RP35 (3468) |
RP55 (7265) |
RP75 (13062) |
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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: | Bateman A |
Previous IDs: | Thr_dehydratase_C; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 12 |
Number in full: | 7645 |
Average length of the domain: | 90.6 aa |
Average identity of full alignment: | 30 % |
Average coverage of the sequence by the domain: | 29.42 % |
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: | 91 | ||||||||||||
Family (HMM) version: | 21 | ||||||||||||
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 Thr_dehydrat_C domain has been found. There are 4 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.