Reviewed,
UniProtKB/Swiss-Prot P23473 (CHLY_PARTH)
Last modified
February 9, 2010.
Version 62.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bifunctional chitinase/lysozyme Including the following 2 domains: 1- Recommended name: Chitinase EC=3.2.1.14 2- Recommended name: Lysozyme EC=3.2.1.17 |
| Organism | Parthenocissus quinquefolia (Virginia creeper) |
| 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 |
| Cellular component | extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cation binding Inferred from electronic annotation. Source: InterPro chitinase activityInferred 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 | |
|---|---|
| SMR | P23473. Positions 1-47. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH18. Glycoside Hydrolase Family 18. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.14. 308047. 3.2.1.17. 308047. |
Family and domain databases | |
| InterPro | IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. 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 project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


