Q70I53 · HDAH_ALCSD

Function

function

Exhibits significant levels of protein deacetylase activity comparable to those of eukaryotic HDACs in assays both with fluorogenic peptidic substrates and acetate-radiolabeled histones. Accepts proteins with epsilon-acetylated lysine residues and tritiated-acetate-prelabeled chicken histones as substrates. The natural substrate protein is not yet known.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Activity regulation

Zinc, and cobalt and nickel at a lesser extent, are able to increase the catalytic activity (2.2-, 1.3- and 1.1-fold respectively) at concentrations of 1 mM. Higher concentrations have an inhibitory effect. Magnesium, manganese and calcium have no effect on activity at concentrations between 0 and 10 mM. At 100 mM, the catalytic activity is increased between 1.2- and 2.1-fold. Hydroxamates like TSA and SAHA inhibit the enzyme (PubMed:15060035).
Is also inhibited by azobenzenes, stilbenes and arylazopyrazoles (PubMed:27756124).

pH Dependence

Optimum pH is 8.0.

Features

Showing features for active site, binding site, site.

TypeIDPosition(s)Description
Active site143Proton donor/acceptor
Binding site180Zn2+ (UniProtKB | ChEBI)
Binding site182Zn2+ (UniProtKB | ChEBI)
Binding site268Zn2+ (UniProtKB | ChEBI)
Site312Polarizes the scissile carbonyl of the substrate

GO annotations

AspectTerm
Molecular Functionhydrolase activity
Molecular Functionmetal ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone deacetylase-like amidohydrolase
  • EC number
  • Short names
    HDAC-like amidohydrolase; HDAH

Gene names

    • Name
      hdaH
    • Synonyms
      hdaH1

Organism names

Accessions

  • Primary accession
    Q70I53

Phenotypes & Variants

Chemistry

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001147282-369Histone deacetylase-like amidohydrolase

Interaction

Subunit

Homotetramer; dimer of dimers.

Chemistry

Family & Domains

Sequence similarities

Belongs to the histone deacetylase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    369
  • Mass (Da)
    39,424
  • Last updated
    2007-01-23 v3
  • Checksum
    25A8C71FFF7C9FE7
MAIGYVWNTLYGWVDTGTGSLAAANLTARMQPISHHLAHPDTKRRFHELVCASGQIEHLTPIAAVAATDADILRAHSAAHLENMKRVSNLPTGGDTGDGITMMGNGGLEIARLSAGGAVELTRRVATGELSAGYALVNPPGHHAPHNAAMGFCIFNNTSVAAGYARAVLGMERVAILDWDVHHGNGTQDIWWNDPSVLTISLHQHLCFPPDSGYSTERGAGNGHGYNINVPLPPGSGNAAYLHAMDQVVLHALRAYRPQLIIVGSGFDASMLDPLARMMVTADGFRQMARRTIDCAADICDGRIVFVQEGGYSPHYLPFCGLAVIEELTGVRSLPDPYHEFLAGMGGNTLLDAERAAIEEIVPLLADIR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ580773
EMBL· GenBank· DDBJ
CAE45336.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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