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P49236 (E13B_BRACM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Glucan endo-1,3-beta-glucosidase

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name=(1->3)-beta-glucanase
Beta-1,3-endoglucanase
Gene names
Name:BGL
OrganismBrassica campestris (Field mustard)
Taxonomic identifier3711 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is thought to be an important plant defense-related product against fungal pathogens. Accumulation of the glucanase can be detected as early as 4 hours after inoculation.

Catalytic activity

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

Subcellular location

Vacuole. Note: In intact tissues.

Induction

Following incompatible or compatible interaction with pathogenic bacteria, but not by wounding or salicylic acid. The induction is localized and does not seem to result from a systemic response. Induction occurs more rapidly with an incompatible interaction.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentVacuole
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

defense response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucan endo-1,3-beta-D-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 By similarity
Chain27 – 342316Glucan endo-1,3-beta-glucosidase
PRO_0000011842

Sites

Active site2611Nucleophile By similarity
Active site3221Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P49236 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 7AE6B1EA445957F7

FASTA34238,180
        10         20         30         40         50         60 
MLASSPMLLF LLSLLMAYNF DTTAGQIGVC FGQMGNNIPN PSEVVAMFKQ YSIPRMRMYG 

        70         80         90        100        110        120 
PNPDALNALR GSNIEFILDV PNGDLKRLAD SQAEANTWVR DNVQKYNDVR FKYISVGNEV 

       130        140        150        160        170        180 
KPGEPGAAAL IQAMQNIDRA LSAAGLSNIK VSTTTFMGPS RNTYPPSRGR FKDEYRNFLQ 

       190        200        210        220        230        240 
PVIGFLVNKR SPLLVNIYTY FGYMNRDVSL QFALLQPNSN NEFTDPNNQL RYLNFFDANL 

       250        260        270        280        290        300 
DSVYAALEKS GGGSLDVVVS ESGWPTQGGP GASVPNAEAY VNNLRLHVNK NGSPKRQEAI 

       310        320        330        340 
ETYIFAMFDE APRQTSPNDE YEKYWGMFSP TTRQLKYGVK FN 

« Hide

References

[1]"Defense-related gene induction in Brassica campestris in response to defined mutants of Xanthomonas campestris with altered pathogenicity."
Newman M.-A., Conrads-Strauch J., Scofield G., Daniels M.J., Dow J.M.
Mol. Plant Microbe Interact. 7:553-563(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 99-117.
Strain: cv. Just Right.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77990 mRNA. Translation: CAA54952.1.
PIRS42885.

3D structure databases

ProteinModelPortalP49236.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE13B_BRACM
AccessionPrimary (citable) accession number: P49236
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries