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P23473 (CHLY_PARTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional chitinase/lysozyme

Including the following 2 domains:

  1. Chitinase
    EC=3.2.1.14
  2. Lysozyme
    EC=3.2.1.17
OrganismParthenocissus quinquefolia (Virginia creeper) (Hedera quinquefolia)
Taxonomic identifier3607 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsVitalesVitaceaeParthenocissus

Protein attributes

Sequence length47 AA.
Sequence statusFragment.
Protein existenceEvidence 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

Secretedextracellular space.

Sequence similarities

Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

polysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchitinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

lysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›47›47Bifunctional chitinase/lysozyme
PRO_0000077052

Experimental info

Non-terminal residue471

Sequences

Sequence LengthMass (Da)Tools
P23473 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 1D9DCF2E7E3A0F51

FASTA475,040
        10         20         30         40 
GGIAIYWGQN GNEGTLTQTC NTGKYSYVNI AFLNKFGNGQ TPEINLA 

« Hide

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

ProteinModelPortalP23473.
SMRP23473. Positions 1-47.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCHLY_PARTH
AccessionPrimary (citable) accession number: P23473
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: February 19, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries