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4  structures 13936  species 2  interactions 20980  sequences 12  architectures

Family: Thr_dehydrat_C (PF00585)

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

  1. 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

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001721

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. Most of the proteins in which it is found are involved in amino acid and purine metabolism:

  • aspartokinases
  • chorismate mutases
  • prephenate dehydrogenases (TyrA)
  • prephenate dehydratases
  • homoserine dehydrogenases
  • malate dehydrogenases
  • phosphoglycerate dehydrogenases
  • phenylalanine and tryptophan-4-monooxygenases
  • phosphoribosylformylglycinamidine synthase (PurQ)
  • uridylyl transferase and removing enzyme (GlnD)
  • GTP pyrophosphokinase/phosphohydrolase (SpoT/RelA)
  • tyrosine and phenol metabolism operon regulators (TyrR)
  • several uncharacterised proteins from archaea, bacteria and plants that contain from one to four copies of this domain [PUBMED:12481063].
  • 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 9 members:

    ACT ACT_3 ACT_4 ACT_5 ACT_6 ACT_7 DUF493 NikR_C Thr_dehydrat_C


    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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics 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.

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    Key: ✓ available, x not generated, not available.

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    Representative proteomes NCBI

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    You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

    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 HMMER3.

    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...


    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 View help on the curation process

    Seed source: Bateman A
    Previous IDs: Thr_dehydratase_C;
    Type: Domain
    Author: Bateman A
    Number in seed: 13
    Number in full: 20980
    Average length of the domain: 91.00 aa
    Average identity of full alignment: 36 %
    Average coverage of the sequence by the domain: 28.73 %

    HMM information View help on HMM parameters

    HMM build commands:
    build method: hmmbuild -o /dev/null HMM SEED
    search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
    Model details:
    Parameter Sequence Domain
    Gathering cut-off 20.8 20.8
    Trusted cut-off 20.8 20.8
    Noise cut-off 20.5 20.5
    Model length: 91
    Family (HMM) version: 14
    Download: download the raw HMM for this family

    Species distribution

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    Colour assignments

    Archea Archea Eukaryota Eukaryota
    Bacteria Bacteria Other sequences Other sequences
    Viruses Viruses Unclassified Unclassified
    Viroids Viroids Unclassified sequence Unclassified sequence


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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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    There are 2 interactions for this family. More...

    PALP Thr_dehydrat_C


    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 seqence.

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