Q5AQQ0 · CDA_EMENI

Function

function

Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate.

Catalytic activity

Cofactor

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Note: Evidence supports a metal cofactor but evidence for cobalt is inconsistent.

Activity regulation

Inhibited by metal chelator ethylenediaminetetraacetic acid (EDTA).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.072 mMGlcNAc5837 in presence of Co2+
kcat is 7 sec-1 with GlcNAc5 as substrate.

pH Dependence

Optimum pH is 8.

Temperature Dependence

Optimum temperature is 50 degrees Celsius.

Features

Showing features for active site, binding site, site.

TypeIDPosition(s)Description
Active site47Proton acceptor
Binding site47acetate (UniProtKB | ChEBI)
Binding site48Co2+ (UniProtKB | ChEBI)
Binding site97Co2+ (UniProtKB | ChEBI)
Binding site101Co2+ (UniProtKB | ChEBI)
Binding site138acetate (UniProtKB | ChEBI)
Site164May prevent de-N-acetylated sugar residues from interacting with the active site
Active site196Proton donor

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionchitin binding
Molecular Functionchitin deacetylase activity
Molecular Functionmetal ion binding
Biological Processcell wall organization
Biological Processchitin catabolic process
Biological Processpolysaccharide catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Chitin deacetylase
  • EC number
  • Alternative names
    • AnCDA

Gene names

    • Name
      cda
    • ORF names
      ANIA_09380

Organism names

Accessions

  • Primary accession
    Q5AQQ0
  • Secondary accessions
    • A0A1U8QU02
    • B3VD86
    • C8VR85

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_501024134219-237Chitin deacetylase
Glycosylation176N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain40-222NodB homology

Sequence similarities

Belongs to the polysaccharide deacetylase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    237
  • Mass (Da)
    26,014
  • Last updated
    2005-04-26 v1
  • Checksum
    16DF188E3D652A3E
MFATLALVFTALASNALTTPLPLVRRVPTGQVITQCTTPNTIALTFDDGPSEYTPQLLDLLSRYSARATFFVLGDAAAQNPGLLQRMRDEGHQVGAHTYDHVSLPSLGYDGIASQMTRLEEVIRPALGVAPAYMRPPYLETNELVLQVMRDLDYRVISASVDTKDYENQDADAIINTSFQLFLDQLDAGGNIVLAHDIHYWTVASLAERMLQEVNARGLIATTVGDCLGDGEIAWYH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EU734183
EMBL· GenBank· DDBJ
ACE79177.1
EMBL· GenBank· DDBJ
mRNA
BN001308
EMBL· GenBank· DDBJ
CBF87506.1
EMBL· GenBank· DDBJ
Genomic DNA
AACD01000172
EMBL· GenBank· DDBJ
EAA66447.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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