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A0A014P1N9 · A0A014P1N9_9BURK

Function

function

NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site51substrate
Binding site54substrate
Binding site86-89NAD+ (UniProtKB | ChEBI)
Active site104Proton acceptor
Binding site117Zn2+ (UniProtKB | ChEBI)
Binding site120Zn2+ (UniProtKB | ChEBI)
Binding site135Zn2+ (UniProtKB | ChEBI)
Binding site138Zn2+ (UniProtKB | ChEBI)
Binding site175-177NAD+ (UniProtKB | ChEBI)
Binding site201-203NAD+ (UniProtKB | ChEBI)
Binding site219NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionNAD+ binding
Molecular FunctionNAD-dependent histone deacetylase activity
Molecular Functionprotein-malonyllysine demalonylase activity
Molecular Functionprotein-succinyllysine desuccinylase activity
Molecular Functiontransferase activity
Molecular Functionzinc ion binding
Biological Processprotein deacetylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NAD-dependent protein deacylase
  • EC number
  • Alternative names
    • Regulatory protein SIR2 homolog

Gene names

    • Name
      cobB
    • ORF names
      AX13_01755

Organism names

  • Taxonomic identifier
  • Strain
    • DA1877
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Comamonas

Accessions

  • Primary accession
    A0A014P1N9

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-234Deacetylase sirtuin-type

Domain

2 residues (Tyr-51 and Arg-54) present in a large hydrophobic pocket are probably involved in substrate specificity. They are important for desuccinylation activity, but dispensable for deacetylation activity.

Sequence similarities

Belongs to the sirtuin family. Class III subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    234
  • Mass (Da)
    24,862
  • Last updated
    2014-06-11 v1
  • MD5 Checksum
    1BC74EF921405E9AA1ED57DC2C8FD264
MTVLTGAGVSAESGVPTFRDVQTGIWAQFDPQEMASEPGFRAHPQRVWQWYAHRRALVSAVQPNAAHRALAQFARHHPGKLQLVTQNVDGLHQRAGSPGVICLHGDLLVHEWLDAVCPQCDLEAAVQRGGEPPSCPACGNPVRPGVVWFGEHLPAAALAQAEAAVQTCDLMLVVGTSGVVYPAAGLVFQAHQQGARVVVVNPDATELDMLADACVRATAAQALPQLLRLDEGCL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JBOK01000010
EMBL· GenBank· DDBJ
EXU80080.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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