Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q01412 (E13A_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. 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 A

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

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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

Secretedextracellular space.

Developmental stage

Maximum expression found during days 4 to 8 and days 8 to 12 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 componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMPyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
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_componentextracellular space

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 – 2323 By similarity
Chain24 – 336313Glucan endo-1,3-beta-glucosidase A
PRO_0000011851

Sites

Active site2571Nucleophile By similarity
Active site3171Proton donor By similarity

Amino acid modifications

Modified residue241Pyrrolidone carboxylic acid Probable

Sequences

Sequence LengthMass (Da)Tools
Q01412 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 5335FDF40DEF9488

FASTA33637,572
        10         20         30         40         50         60 
MAFLSSLLAS LLLVGLLIQI TGAQPIGVCY GKIANNLPSD QDVIKLYNSN NIKKMRIYFP 

        70         80         90        100        110        120 
ETNVFNALKG SNIEIILDVP NQDLEALANP SKRQGWVQDN IRNHFPDVKF KYIAVGNEVD 

       130        140        150        160        170        180 
PGRDSGKYAR FVGPAMENIY NALSSAGLQN QIKVSTATYL GLLTNTYPPR DSIFRDEYKS 

       190        200        210        220        230        240 
FINPIIGFLS RHNLPLLANI YPYFGHADDN VPLPYALFKQ QGLNDAGYQN LFDALVDSMY 

       250        260        270        280        290        300 
FATEKLGGQN IEIIVSESGW PSEGHPSATL ENAMTYYTNL INHVKGGAGT PKKPGRTIET 

       310        320        330 
YLFAMFDENR KDGKPSEQHF GLFKPDQRPK YQLKFD 

« Hide

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], PROTEIN SEQUENCE OF 312-330.
Strain: cv. Moneymaker.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80604 mRNA. Translation: AAA03617.1.
PIRS26240.
RefSeqNP_001234798.1. NM_001247869.1.
UniGeneLes.3673.

3D structure databases

ProteinModelPortalQ01412.
SMRQ01412. Positions 26-335.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome2549. Sola l Glucanase.
CAZyGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID543986.
KEGGsly:543986.

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 nameE13A_SOLLC
AccessionPrimary (citable) accession number: Q01412
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 19, 2014
This is version 79 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