P93159 · ENG1_SOYBN

Function

function

Cleaves internal linkages in 1,3-beta-glucan (PubMed:14578352, PubMed:16297387).
Beta-glucan, a polysaccharide constituent of fungal cell walls, can act as an elicitor in the plant, triggering defense responses including phytoalexin synthesis (PubMed:9023377).

Catalytic activity

  • Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
    EC:3.2.1.39 (UniProtKB | ENZYME | Rhea)

Features

Showing features for site, active site, binding site.

166850100150200250300350400450500550600650
TypeIDPosition(s)Description
Site7Not glycosylated
Active site418
Binding site422(1,3-beta-D-glucosyl)n (UniProtKB | ChEBI)
Active site494
Binding site494(1,3-beta-D-glucosyl)n (UniProtKB | ChEBI)
Active site498
Binding site498(1,3-beta-D-glucosyl)n (UniProtKB | ChEBI)
Site636Not glycosylated

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componentplant-type cell wall
Molecular Functionglucan endo-1,3-beta-D-glucosidase activity
Molecular Functionglucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group
Molecular Functionglucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group
Molecular Functionpolysaccharide binding
Biological Processcell wall organization
Biological Processcell wall polysaccharide catabolic process
Biological Processdetection of symbiotic fungus

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Glucan endo-1,3-beta-D-glucosidase
  • EC number
  • Short names
    Endo-1,3-beta-glucanase
  • Alternative names
    • Beta-glucan elicitor-binding protein
      (GEBP
      )
    • Laminarinase

Gene names

    • Name
      GBP

Organism names

  • Taxonomic identifier
  • Strains
    • Green Homer
    • cv. 9007
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Glycine > Glycine subgen. Soja

Accessions

  • Primary accession
    P93159
  • Secondary accessions
    • Q9FST0

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis494-498Loss of enzyme activity.

PTM/Processing

Features

Showing features for initiator methionine, chain, glycosylation.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00004570722-668Glucan endo-1,3-beta-D-glucosidase
Glycosylation65N-linked (GlcNAc...) asparagine
Glycosylation124N-linked (GlcNAc...) asparagine
Glycosylation160N-linked (GlcNAc...) asparagine
Glycosylation187N-linked (GlcNAc...) asparagine
Glycosylation465N-linked (GlcNAc...) asparagine

Keywords

Expression

Tissue specificity

Expressed in roots (at protein level) (PubMed:11030428, PubMed:14578352, PubMed:9023377).
Expressed in leaves (PubMed:9023377).

Gene expression databases

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region2-208beta-sandwich subdomain
Domain2-668GH81
Region209-299alpha/beta subdomain
Region240-443Involved in beta-glucan binding
Region309-668(alpha/beta)6 barrel subdomain
Region564-566May provide specificity for triple-helical beta-glucan

Sequence similarities

Belongs to the glycosyl hydrolase 81 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    668
  • Mass (Da)
    74,610
  • Last updated
    2001-12-01 v2
  • Checksum
    0D6992870BFC481E
MVNIQTNTSYIFPQTQSTVLPDPSKFFSSNLLSSPLPTNSFFQNFVLKNGDQQEYIHPYLIKSSNSSLSLSYPSRQASSAVIFQVFNPDLTISAPQGPKQGPPGKHLISSYSDLSVTLDFPSSNLSFFLVRGSPYLTVSVTQPTPLSITTIHSILSFSSNDSNTKYTFQFNNGQTWLLYATSPIKLNHTLSEITSNAFSGIIRIALLPDSDSKHEAVLDKYSSCYPVSGKAVFREPFCVEYNWEKKDSGDLLLLAHPLHVQLLRNGDNDVKILEDLKYKSIDGDLVGVVGDSWVLKTDPLFVTWHSIKGIKEESHDEIVSALSKDVESLDSSSITTTESYFYGKLIARAARLVLIAEELNYPDVIPKVRNFLKETIEPWLEGTFSGNGFLHDEKWGGIITQKGSTDAGGDFGFGIYNDHHYHLGYFIYGIAVLTKLDPAWGRKYKPQAYSIVQDFLNLDTKLNSNYTRLRCFDPYVLHSWAGGLTEFTDGRNQESTSEAVSAYYSAALMGLAYGDAPLVALGSTLTALEIEGTKMWWHVKEGGTLYEKEFTQENRVMGVLWSNKRDTGLWFAPAEWKECRLGIQLLPLAPISEAIFSNVDFVKELVEWTLPALDREGGVGEGWKGFVYALEGVYDNESALQKIRNLKGFDGGNSLTNLLWWIHSRSDE

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict149in Ref. 2; CAA71307
Sequence conflict516in Ref. 2; CAA71307

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D78510
EMBL· GenBank· DDBJ
BAA11407.1
EMBL· GenBank· DDBJ
mRNA
Y10257
EMBL· GenBank· DDBJ
CAA71307.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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