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Protein

Chitosanase

Gene

csn

Organism
Bacillus circulans
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei79 – 791Proton donorPROSITE-ProRule annotation
Active sitei97 – 971NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17652.
BRENDAi3.2.1.132. 649.

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
OrganismiBacillus circulans
Taxonomic identifieri1397 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

DrugBankiDB01296. Glucosamine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242Add
BLAST
Chaini43 – 301259ChitosanasePRO_0000012206Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi92 ↔ 166

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
301
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 484Combined sources
Helixi51 – 6111Combined sources
Helixi65 – 8016Combined sources
Helixi85 – 906Combined sources
Beta strandi96 – 994Combined sources
Turni104 – 1074Combined sources
Beta strandi115 – 1173Combined sources
Helixi125 – 1306Combined sources
Helixi138 – 1447Combined sources
Beta strandi149 – 1524Combined sources
Beta strandi155 – 1584Combined sources
Helixi162 – 1709Combined sources
Helixi171 – 1744Combined sources
Helixi176 – 18914Combined sources
Helixi191 – 1999Combined sources
Helixi206 – 21914Combined sources
Beta strandi221 – 2244Combined sources
Helixi228 – 2336Combined sources
Helixi241 – 25616Combined sources
Turni259 – 2613Combined sources
Helixi266 – 27914Combined sources
Helixi289 – 2957Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QGIX-ray1.60A43-301[»]
2D05X-ray2.00A43-301[»]
ProteinModelPortaliP33673.
SMRiP33673. Positions 43-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33673.

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.

P33673-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHMSNARPSK SRTKFLLAFL CFTLMASLFG ATALFGPSKA AAASPDDNFS
60 70 80 90 100
PETLQFLRNN TGLDGEQWNN IMKLINKPEQ DDLNWIKYYG YCEDIEDERG
110 120 130 140 150
YTIGLFGATT GGSRDTHPDG PDLFKAYDAA KGASNPSADG ALKRLGINGK
160 170 180 190 200
MKGSILEIKD SEKVFCGKIK KLQNDAAWRK AMWETFYNVY IRYSVEQARQ
210 220 230 240 250
RGFTSAVTIG SFVDTALNQG ATGGSDTLQG LLARSGSSSN EKTFMKNFHA
260 270 280 290 300
KRTLVVDTNK YNKPPNGKNR VKQWDTLVDM GKMNLKNVDS EIAQVTDWEM

K
Length:301
Mass (Da):33,426
Last modified:March 1, 2004 - v2
Checksum:i5B67FB8FF1D1F763
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10624 Genomic DNA. Translation: BAA01474.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10624 Genomic DNA. Translation: BAA01474.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QGIX-ray1.60A43-301[»]
2D05X-ray2.00A43-301[»]
ProteinModelPortaliP33673.
SMRiP33673. Positions 43-301.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB01296. Glucosamine.

Protein family/group databases

CAZyiGH46. Glycoside Hydrolase Family 46.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17652.
BRENDAi3.2.1.132. 649.

Miscellaneous databases

EvolutionaryTraceiP33673.

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]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of chitosanase produced by Bacillus circulans MH-K1."
    Ando A., Noguchi K., Yanagi M., Shinoyama H., Kagawa Y., Hirata H., Yabuki M., Fujii T.
    J. Gen. Appl. Microbiol. 38:135-144(1992)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: MH-K1.
  2. Ando A.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 119-124; 140 AND 200-202.
  3. "Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism."
    Saito J., Kita A., Higuchi Y., Nagata Y., Ando A., Miki K.
    J. Biol. Chem. 274:30818-30825(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 43-301.
    Strain: MH-K1.

Entry informationi

Entry nameiCHIS_BACCI
AccessioniPrimary (citable) accession number: P33673
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: March 1, 2004
Last modified: December 9, 2015
This is version 82 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.