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Q01413 (E13B_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. 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 B

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase B
Short name=(1->3)-beta-glucanase B
Basic beta-1,3-glucanase
Beta-1,3-endoglucanase B
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum) [Reference proteome]
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Implicated in the defense of plants against pathogens.

Catalytic activity

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

Subcellular location

Vacuole Potential.

Developmental stage

Maximum expression found during days 4 to 6 and days 4 to 14 after inoculation with an avirulent and a virulent pathogen respectively.

Induction

Upon infection by virulent and avirulent races of pathogens, for example fungal pathogen C.fulvum.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentVacuole
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Reference proteome
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 By similarity
Chain26 – 340315Glucan endo-1,3-beta-glucosidase B
PRO_0000011852
Propeptide341 – 36020Removed in mature form Probable
PRO_0000011853

Sites

Active site2651Nucleophile By similarity
Active site3211Proton donor By similarity

Amino acid modifications

Modified residue261Pyrrolidone carboxylic acid Probable
Glycosylation3501N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q01413 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: EB29C1AB76347EE1

FASTA36039,719
        10         20         30         40         50         60 
MATSQIAIIV LLGLLVATNI HITEAQIGVC YGMMGNNLPS HSEVIQLYKS RNIRRLRLYD 

        70         80         90        100        110        120 
PNHGALNALR GSNIEVILGL PNVDVKHISS GMEHARWWVQ KNVRDFWPHV KIKYIAVGNE 

       130        140        150        160        170        180 
ISPVTGTSNL APFQVPALVN IYKAIGEAGL GNDIKVSTSV DMTLIGNSYP PSQGSFRNDV 

       190        200        210        220        230        240 
RWFTDPIVGF LRDTRAPLLV NIYPYFSYSG NPGQISLPYA LFTAPNVVVQ DGSRQYRNLF 

       250        260        270        280        290        300 
DAMLDSVYAA MDRTGGGSVG IVVSESGWPS AGAFGATHEN AQTYLRNLIQ HAKEGSPRKP 

       310        320        330        340        350        360 
GPIETYIFAM FDENNKNPEL EKHFGMFSPN KQPKYNLNFG VSERVWDITN STASSLTSEI 

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References

[1]"Differential accumulation of mRNAs encoding extracellular and intracellular PR proteins in tomato induced by virulent and avirulent races of Cladosporium fulvum."
van Kan J.A.L., Joosten M.H.A.J., Wagemakers C.A.M., van den Berg-Velthuis G.C.M., de Wit P.J.G.M.
Plant Mol. Biol. 20:513-527(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Moneymaker.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80608 mRNA. Translation: AAA03618.1.
PIRS26241.
RefSeqNP_001234805.1. NM_001247876.1.
UniGeneLes.8987.

3D structure databases

ProteinModelPortalQ01413.
SMRQ01413. Positions 27-339.
ModBaseSearch...

Protein family/group databases

Allergome2549. Lyc e Glucanase.
CAZyGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsSolyc01g059980.2.1; Solyc01g059980.2.1; Solyc01g059980.2.
Solyc01g060020.2.1; Solyc01g060020.2.1; Solyc01g060020.2.
GeneID543987.

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. Glyco_hydro_cat. 1 hit.
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE13B_SOLLC
AccessionPrimary (citable) accession number: Q01413
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families