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P33665 (CHIS_STRSN) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Chitosanase

EC=3.2.1.132
Gene names
Name:csn
Synonyms:chs
OrganismStreptomyces sp. (strain N174)
Taxonomic identifier69019 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Aids in the defense against invading fungal pathogens by degrading their cell wall chitosan.

Catalytic activity

Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 46 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchitosanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4040 Ref.2
Chain41 – 278238Chitosanase
PRO_0000012209

Sites

Active site621Proton donor
Active site801Nucleophile

Experimental info

Mutagenesis621E → D or Q: Drastic reduction of activity.
Mutagenesis801D → E or N: Drastic reduction of activity.

Secondary structure

.............................................. 278
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33665 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: AEB36286AA9AF95F

FASTA27829,835
        10         20         30         40         50         60 
MHSQHRTARI ALAVVLTAIP ASLATAGVGY ASTQASTAVK AGAGLDDPHK KEIAMELVSS 

        70         80         90        100        110        120 
AENSSLDWKA QYKYIEDIGD GRGYTGGIIG FCSGTGDMLE LVQHYTDLEP GNILAKYLPA 

       130        140        150        160        170        180 
LKKVNGSASH SGLGTPFTKD WATAAKDTVF QQAQNDERDR VYFDPAVSQA KADGLRALGQ 

       190        200        210        220        230        240 
FAYYDAIVMH GPGNDPTSFG GIRKTAMKKA RTPAQGGDET TYLNAFLDAR KAAMLTEAAH 

       250        260        270 
DDTSRVDTEQ RVFLKAGNLD LNPPLKWKTY GDPYVINS 

« Hide

References

[1]"Primary sequence of the chitosanase from Streptomyces sp. strain N174 and comparison with other endoglycosidases."
Masson J.-Y., Denis F., Brzezinski R.
Gene 140:103-107(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Purification and characterization of a chitosanase from Streptomyces N174."
Boucher I., Dupuy A., Vidal P., Neugebauer W.A., Brzezinski R.
Appl. Microbiol. Biotechnol. 38:188-193(1992)
Cited for: PROTEIN SEQUENCE OF 41-57, CHARACTERIZATION.
[3]"Cloning and expression in Streptomyces lividans of a chitanase-encoding gene from the actinomycete Kitasatosporia N174 isolated from soil."
Fink D., Boucher I., Denis F., Brzezinski R.
Biotechnol. Lett. 13:845-850(1991)
Cited for: CHARACTERIZATION.
[4]"Reaction mechanism of chitosanase from Streptomyces sp. N174."
Fukamizo T., Honda Y., Goto S., Boucher I., Brzezinski R.
Biochem. J. 311:377-383(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Site-directed mutagenesis of evolutionary conserved carboxylic amino acids in the chitosanase from Streptomyces sp. N174 reveals two residues essential for catalysis."
Boucher I., Fukamizo T., Honda Y., Willick G.E., Neugebauer W.A., Brzezinski R.
J. Biol. Chem. 270:31077-31082(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[6]"X-ray structure of an anti-fungal chitosanase from streptomyces N174."
Marcotte E.M., Monzingo A.F., Ernst S.R., Brzezinski R., Robertus J.D.
Nat. Struct. Biol. 3:155-162(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07779 Genomic DNA. Translation: AAA19865.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CHKX-ray2.40A/B41-278[»]
ProteinModelPortalP33665.
SMRP33665. Positions 41-278.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH46. Glycoside Hydrolase Family 46.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP33665.

Family and domain databases

Gene3D3.30.386.10. 1 hit.
InterProIPR000400. Glyco_hydro_46.
IPR023099. Glyco_hydro_46_N.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF01374. Glyco_hydro_46. 1 hit.
[Graphical view]
PIRSFPIRSF036551. Chitosanase. 1 hit.
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS60000. CHITOSANASE_46_80. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33665.

Entry information

Entry nameCHIS_STRSN
AccessionPrimary (citable) accession number: P33665
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 16, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries