Q06702 · CDA1_YEAST
- ProteinChitin deacetylase 1
- GeneCDA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids301 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate (PubMed:9133736).
Chitosan is a component of the spore wall (PubMed:9133736).
Chitosan is a component of the spore wall (PubMed:9133736).
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
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 115 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 115 | acetate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 116 | Co2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 162 | Co2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 166 | Co2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 203 | acetate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 263 | Proton donor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | prospore membrane | |
Molecular Function | chitin binding | |
Molecular Function | chitin deacetylase activity | |
Molecular Function | metal ion binding | |
Biological Process | ascospore wall assembly | |
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 1
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ06702
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MKIFNTIQSVLFAAFFLKQGNCLA | ||||||
Chain | PRO_0000024826 | 25-301 | Chitin deacetylase 1 | |||
Sequence: SNGSTALMGEVDMQTPFPEWLTEFTNLTQWPGIDPPYIPLDYINLTEVPELDRYYPGQCPKISREQCSFDCYNCIDVDDVTSCFKLSQTFDDGPAPATEALLKKLRQRTTFFVLGINTVNYPDIYEHILERGHLIGTHTWSHEFLPSLSNEEIVAQIEWSIWAMNATGKHFPKYFRPPYGAIDNRVRAIVKQFGLTVVLWDLDTFDWKLITNDDFRTEEEILMDINTWKGKRKGLILEHDGARRTVEVAIKINELIGSDQLTIAECIGDTDYIERYD | ||||||
Glycosylation | 26 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 50 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 68 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 107↔290 | |||||
Sequence: CFKLSQTFDDGPAPATEALLKKLRQRTTFFVLGINTVNYPDIYEHILERGHLIGTHTWSHEFLPSLSNEEIVAQIEWSIWAMNATGKHFPKYFRPPYGAIDNRVRAIVKQFGLTVVLWDLDTFDWKLITNDDFRTEEEILMDINTWKGKRKGLILEHDGARRTVEVAIKINELIGSDQLTIAEC | ||||||
Glycosylation | 189 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Induced during sporulation.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 108-288 | NodB homology | ||||
Sequence: FKLSQTFDDGPAPATEALLKKLRQRTTFFVLGINTVNYPDIYEHILERGHLIGTHTWSHEFLPSLSNEEIVAQIEWSIWAMNATGKHFPKYFRPPYGAIDNRVRAIVKQFGLTVVLWDLDTFDWKLITNDDFRTEEEILMDINTWKGKRKGLILEHDGARRTVEVAIKINELIGSDQLTIA |
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.
- Length301
- Mass (Da)34,642
- Last updated1996-11-01 v1
- Checksum72FEB92E5BF5E252
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U17247 EMBL· GenBank· DDBJ | AAB67356.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY557948 EMBL· GenBank· DDBJ | AAS56274.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09616.1 EMBL· GenBank· DDBJ | Genomic DNA |