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P33665

- CHIS_STRSN

UniProt

P33665 - CHIS_STRSN

Protein

Chitosanase

Gene

csn

Organism
Streptomyces sp. (strain N174)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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

    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-SubCell

    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

    MHSQHRTARI ALAVVLTAIP ASLATAGVGY ASTQASTAVK AGAGLDDPHK    50
    KEIAMELVSS AENSSLDWKA QYKYIEDIGD GRGYTGGIIG FCSGTGDMLE 100
    LVQHYTDLEP GNILAKYLPA LKKVNGSASH SGLGTPFTKD WATAAKDTVF 150
    QQAQNDERDR VYFDPAVSQA KADGLRALGQ FAYYDAIVMH GPGNDPTSFG 200
    GIRKTAMKKA RTPAQGGDET TYLNAFLDAR KAAMLTEAAH DDTSRVDTEQ 250
    RVFLKAGNLD LNPPLKWKTY GDPYVINS 278
    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 1, 2014
    This is version 67 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