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P33665

- CHIS_STRSN

UniProt

P33665 - CHIS_STRSN

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Protein

Chitosanase

Gene

csn

Organism
Streptomyces sp. (strain N174)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei62 – 621Proton donor
Active sitei80 – 801Nucleophile

GO - Molecular functioni

  1. chitosanase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

SABIO-RKP33665.

Protein family/group databases

CAZyiGH46. Glycoside Hydrolase Family 46.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitosanase (EC:3.2.1.132)
Gene namesi
Name:csn
Synonyms:chs
OrganismiStreptomyces sp. (strain N174)
Taxonomic identifieri69019 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 621E → D or Q: Drastic reduction of activity. 1 Publication
Mutagenesisi80 – 801D → E or N: Drastic reduction of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 40401 PublicationAdd
BLAST
Chaini41 – 278238ChitosanasePRO_0000012209Add
BLAST

Structurei

Secondary structure

1
278
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 463
Helixi48 – 6215
Beta strandi63 – 664
Helixi68 – 714
Beta strandi75 – 773
Beta strandi79 – 824
Beta strandi84 – 863
Turni87 – 904
Turni93 – 953
Helixi97 – 10812
Helixi115 – 1173
Helixi118 – 1247
Helixi134 – 14411
Helixi148 – 16114
Helixi163 – 17210
Helixi177 – 19014
Beta strandi192 – 1954
Helixi199 – 20911
Helixi213 – 2153
Helixi219 – 23618
Helixi244 – 2474
Helixi250 – 2556
Beta strandi265 – 2695
Beta strandi272 – 2765

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CHKX-ray2.40A/B41-278[»]
ProteinModelPortaliP33665.
SMRiP33665. Positions 41-278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33665.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 46 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.30.386.10. 1 hit.
InterProiIPR000400. Glyco_hydro_46.
IPR023099. Glyco_hydro_46_N.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF01374. Glyco_hydro_46. 1 hit.
[Graphical view]
PIRSFiPIRSF036551. Chitosanase. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS60000. CHITOSANASE_46_80. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33665-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHSQHRTARI ALAVVLTAIP ASLATAGVGY ASTQASTAVK AGAGLDDPHK
60 70 80 90 100
KEIAMELVSS AENSSLDWKA QYKYIEDIGD GRGYTGGIIG FCSGTGDMLE
110 120 130 140 150
LVQHYTDLEP GNILAKYLPA LKKVNGSASH SGLGTPFTKD WATAAKDTVF
160 170 180 190 200
QQAQNDERDR VYFDPAVSQA KADGLRALGQ FAYYDAIVMH GPGNDPTSFG
210 220 230 240 250
GIRKTAMKKA RTPAQGGDET TYLNAFLDAR KAAMLTEAAH DDTSRVDTEQ
260 270
RVFLKAGNLD LNPPLKWKTY GDPYVINS
Length:278
Mass (Da):29,835
Last modified:February 1, 1994 - v1
Checksum:iAEB36286AA9AF95F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07779 Genomic DNA. Translation: AAA19865.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07779 Genomic DNA. Translation: AAA19865.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CHK X-ray 2.40 A/B 41-278 [» ]
ProteinModelPortali P33665.
SMRi P33665. Positions 41-278.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH46. Glycoside Hydrolase Family 46.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P33665.

Miscellaneous databases

EvolutionaryTracei P33665.

Family and domain databases

Gene3Di 3.30.386.10. 1 hit.
InterProi IPR000400. Glyco_hydro_46.
IPR023099. Glyco_hydro_46_N.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF01374. Glyco_hydro_46. 1 hit.
[Graphical view ]
PIRSFi PIRSF036551. Chitosanase. 1 hit.
SUPFAMi SSF53955. SSF53955. 1 hit.
PROSITEi PS60000. CHITOSANASE_46_80. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiCHIS_STRSN
AccessioniPrimary (citable) accession number: P33665
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 29, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3