P23473 (CHLY_PARTH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 71.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Bifunctional chitinase/lysozyme |
| Organism | Parthenocissus quinquefolia (Virginia creeper) (Hedera quinquefolia) |
| Taxonomic identifier | 3607 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › Vitales › Vitaceae › Parthenocissus![]() |
Protein attributes
| Sequence length | 47 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Bifunctional enzyme with lysozyme/chitinase activity. |
| Catalytic activity | Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Chitin degradation Polysaccharide degradation |
| Cellular component | Secreted |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Direct protein sequencing Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological_process | chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | chitinase activity Inferred from electronic annotation. Source: EC lysozyme activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Purification and N-terminal amino-acid sequence of a basic lysozyme from Parthenocissus quinquifolia cultured in vitro." Bernasconi P., Locher R., Pilet P.E., Jolles J., Jolles P. Biochim. Biophys. Acta 915:254-260(1987) Cited for: PROTEIN SEQUENCE. |
Cross-references
3D structure databases | |
|---|---|
| ProteinModelPortal | P23473. |
| SMR | P23473. Positions 1-47. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH18. Glycoside Hydrolase Family 18. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.20.20.80. 1 hit. |
| InterPro | IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| PROSITE | PS01095. CHITINASE_18. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CHLY_PARTH | ||||||||
| Accession | Primary (citable) accession number: P23473 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
