Q5AQQ0 · CDA_EMENI
- ProteinChitin deacetylase
- Genecda
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids237 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate.
Catalytic activity
- [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosanThis reaction proceeds in the forward direction.
[(1→4)-N-acetyl-β-D-glucosaminyl](n) RHEA-COMP:9593 + n CHEBI:15377 = n CHEBI:30089 + chitosan RHEA-COMP:9597
Cofactor
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 mM | GlcNAc5 | 8 | 37 | 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 47 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 47 | acetate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 48 | Co2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 97 | Co2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 101 | Co2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 138 | acetate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Site | 164 | May prevent de-N-acetylated sugar residues from interacting with the active site | ||||
Sequence: K | ||||||
Active site | 196 | Proton donor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | chitin binding | |
Molecular Function | chitin deacetylase activity | |
Molecular Function | metal ion binding | |
Biological Process | cell wall organization | |
Biological Process | chitin catabolic process | |
Biological Process | polysaccharide catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChitin deacetylase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes
Accessions
- Primary accessionQ5AQQ0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MFATLALVFTALASNALT | ||||||
Chain | PRO_5010241342 | 19-237 | Chitin deacetylase | |||
Sequence: TPLPLVRRVPTGQVITQCTTPNTIALTFDDGPSEYTPQLLDLLSRYSARATFFVLGDAAAQNPGLLQRMRDEGHQVGAHTYDHVSLPSLGYDGIASQMTRLEEVIRPALGVAPAYMRPPYLETNELVLQVMRDLDYRVISASVDTKDYENQDADAIINTSFQLFLDQLDAGGNIVLAHDIHYWTVASLAERMLQEVNARGLIATTVGDCLGDGEIAWYH | ||||||
Glycosylation | 176 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 40-222 | NodB homology | ||||
Sequence: NTIALTFDDGPSEYTPQLLDLLSRYSARATFFVLGDAAAQNPGLLQRMRDEGHQVGAHTYDHVSLPSLGYDGIASQMTRLEEVIRPALGVAPAYMRPPYLETNELVLQVMRDLDYRVISASVDTKDYENQDADAIINTSFQLFLDQLDAGGNIVLAHDIHYWTVASLAERMLQEVNARGLIAT |
Sequence similarities
Belongs to the polysaccharide deacetylase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length237
- Mass (Da)26,014
- Last updated2005-04-26 v1
- Checksum16DF188E3D652A3E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |