P0CP76 · CDA3_CRYNJ
- ProteinChitin deacetylase 3
- GeneCDA3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids410 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate (By similarity).
Chitosan is required to anchor melanin to the cell wall, for maintenance of cell wall integrity, and for proper cytokinesis (By similarity).
Chitosan offers an advantage during infection as it is less readily detected than chitin by host immunosurveillance mechanisms (By similarity).
Chitosan is required to anchor melanin to the cell wall, for maintenance of cell wall integrity, and for proper cytokinesis (By similarity).
Chitosan offers an advantage during infection as it is less readily detected than chitin by host immunosurveillance mechanisms (By similarity).
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 | 131 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 131 | acetate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 132 | Co2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 183 | Co2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 187 | Co2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 225 | acetate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 289 | Proton donor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
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 | fungal-type cell wall biogenesis | |
Biological Process | polysaccharide catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChitin deacetylase 3
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus > Cryptococcus neoformans species complex
Accessions
- Primary accessionP0CP76
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 22 | in strain: CAP 67 | ||||
Sequence: P → H | ||||||
Natural variant | 219 | in strain: CAP 67 | ||||
Sequence: M → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
Miscellaneous
PTM/Processing
Features
Showing features for signal, propeptide, chain, glycosylation, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MYGHLSLSTLSLLAVVAA | ||||||
Propeptide | PRO_0000024828 | 19-39 | ||||
Sequence: APFPESWLQPRDSDVSQLFRR | ||||||
Chain | PRO_0000024829 | 40-385 | Chitin deacetylase 3 | |||
Sequence: GAPDPKASDYLSYYPSPGSTPNVSTIPQAWLDKLATVQLPNVSVATANDGRPTYPNNENDGDSEICSFTDQCYVEDDLYSPPGEKVWALSFDDGPTDVSPALYDYLAQNNISSSATHFMIGGNIITSPQSVLIAIEAGGHLAVHTWSHPYMTTLTNEQVVAELGWTMQALSDLNGGRIPMYWRPPYGDVDNRVRAIAKGVFGLVTVLWDSDTNDWAISDQPDQYSVASVEAYFDTLVTGNRTQGLLLLEHELDNNTVEVFETEYPKAVANGWSVKNVADAFSMKWYLNSGKGNDDVVTTMSVAGTLTTAKPTHTSTSVASATATSSASVTDSAGVSIASAASSQES | ||||||
Glycosylation | 61 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 80 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 149 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 279 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 293 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 385 | GPI-anchor amidated serine | ||||
Sequence: S | ||||||
Propeptide | PRO_0000451829 | 386-410 | Removed in mature form | |||
Sequence: SSWPIANRPSLFVIACGLALAAIMV |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 124-314 | NodB homology | ||||
Sequence: KVWALSFDDGPTDVSPALYDYLAQNNISSSATHFMIGGNIITSPQSVLIAIEAGGHLAVHTWSHPYMTTLTNEQVVAELGWTMQALSDLNGGRIPMYWRPPYGDVDNRVRAIAKGVFGLVTVLWDSDTNDWAISDQPDQYSVASVEAYFDTLVTGNRTQGLLLLEHELDNNTVEVFETEYPKAVANGWSVK |
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.
- Length410
- Mass (Da)43,971
- Last updated2011-06-28 v1
- Checksum73338AC415E2771A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ938050 EMBL· GenBank· DDBJ | CAI79614.1 EMBL· GenBank· DDBJ | mRNA | ||
AE017344 EMBL· GenBank· DDBJ | AAW42893.1 EMBL· GenBank· DDBJ | Genomic DNA |