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Reviewed, UniProtKB/Swiss-Prot P36910 (CHIE_BETVU)

Last modified September 22, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acidic endochitinase SE2
    EC=3.2.1.14
Gene names
Name: SE2
OrganismBeta vulgaris (Sugar beet)
Taxonomic identifier161934 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesAmaranthaceaeBeta

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This protein functions as a defense against chitin containing fungal pathogens. This endochitinase also exhibits exochitinase activity, i.e., it is capable of hydrolyzing chito-oligosaccharides, including chitobiose.

Catalytic activity

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

Subcellular location

Secretedextracellular space. Note: Intercellular fluid of leaves.

Tissue specificity

Accumulates in leaves during infection.

Induction

By fungal infection.

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Chitin degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

chitinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 293268Acidic endochitinase SE2
PRO_0000011914

Sites

Active site1511Proton donor By similarity

Amino acid modifications

Disulfide bond45 ↔ 91 By similarity
Disulfide bond75 ↔ 81 By similarity
Disulfide bond183 ↔ 212 By similarity

Sequences

Sequence LengthMass (Da)Tools
P36910-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 0E9019D28FD34123

FASTA29330,729
        10         20         30         40         50         60 
MAAKIVSVLF LISLLIFASF ESSHGSQIVI YWGQNGDEGS LADTCNSGNY GTVILAFVAT 

        70         80         90        100        110        120 
FGNGQTPALN LAGHCDPATN CNSLSSDIKT CQQAGIKVLL SIGGGAGGYS LSSTDDANTF 

       130        140        150        160        170        180 
ADYLWNTYLG GQSSTRPLGD AVLDGIDFDI ESGDGRFWDD LARALAGHNN GQKTVYLSAA 

       190        200        210        220        230        240 
PQCPLPDASL STAIATGLFD YVWVQFYNNP PCQYDTSADN LLSSWNQWTT VQANQIFLGL 

       250        260        270        280        290 
PASTDAAGSG FIPADALTSQ VLPTIKGSAK YGGVMLWSKA YDSGYSSAIK SSV 

« Hide

References

[1]"An acidic class III chitinase in sugar beet: induction by Cercospora beticola, characterization, and expression in transgenic tobacco plants."
Nielsen K.K., Mikkelsen J.D., Kragh K.M., Bojsen K.
Mol. Plant Microbe Interact. 6:495-506(1993) [PubMed: 8400378] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Monova.
Tissue: Leaf.

Cross-references

Sequence databases

S66038 mRNA. Translation: AAB28479.1.

3D structure databases

HSSPHSSP built from PDB template 2HVM based on UniProtKB P23472.
ModBaseSearch...

Protein family/group databases

CAZyGH18. Glycoside Hydrolase Family 18.

Enzyme and pathway databases

BRENDA3.2.1.14. 124.

Family and domain databases

InterProIPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
PROSITEPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHIE_BETVU
AccessionPrimary (citable) accession number: P36910
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 22, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents