P93159 · ENG1_SOYBN
- ProteinGlucan endo-1,3-beta-D-glucosidase
- GeneGBP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids668 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 7 | Not glycosylated | ||||
Sequence: N | ||||||
Active site | 418 | |||||
Sequence: D | ||||||
Binding site | 422 | (1,3-beta-D-glucosyl)n (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 494 | |||||
Sequence: E | ||||||
Binding site | 494 | (1,3-beta-D-glucosyl)n (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 498 | |||||
Sequence: E | ||||||
Binding site | 498 | (1,3-beta-D-glucosyl)n (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Site | 636 | Not glycosylated | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plant-type cell wall | |
Molecular Function | glucan endo-1,3-beta-D-glucosidase activity | |
Molecular Function | glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group | |
Molecular Function | glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group | |
Molecular Function | polysaccharide binding | |
Biological Process | cell wall organization | |
Biological Process | cell wall polysaccharide catabolic process | |
Biological Process | detection of symbiotic fungus |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlucan endo-1,3-beta-D-glucosidase
- EC number
- Short namesEndo-1,3-beta-glucanase
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > 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 accessionP93159
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 494-498 | Loss of enzyme activity. | ||||
Sequence: ESTSE → QSTSQ |
PTM/Processing
Features
Showing features for initiator methionine, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000457072 | 2-668 | Glucan endo-1,3-beta-D-glucosidase | |||
Sequence: VNIQTNTSYIFPQTQSTVLPDPSKFFSSNLLSSPLPTNSFFQNFVLKNGDQQEYIHPYLIKSSNSSLSLSYPSRQASSAVIFQVFNPDLTISAPQGPKQGPPGKHLISSYSDLSVTLDFPSSNLSFFLVRGSPYLTVSVTQPTPLSITTIHSILSFSSNDSNTKYTFQFNNGQTWLLYATSPIKLNHTLSEITSNAFSGIIRIALLPDSDSKHEAVLDKYSSCYPVSGKAVFREPFCVEYNWEKKDSGDLLLLAHPLHVQLLRNGDNDVKILEDLKYKSIDGDLVGVVGDSWVLKTDPLFVTWHSIKGIKEESHDEIVSALSKDVESLDSSSITTTESYFYGKLIARAARLVLIAEELNYPDVIPKVRNFLKETIEPWLEGTFSGNGFLHDEKWGGIITQKGSTDAGGDFGFGIYNDHHYHLGYFIYGIAVLTKLDPAWGRKYKPQAYSIVQDFLNLDTKLNSNYTRLRCFDPYVLHSWAGGLTEFTDGRNQESTSEAVSAYYSAALMGLAYGDAPLVALGSTLTALEIEGTKMWWHVKEGGTLYEKEFTQENRVMGVLWSNKRDTGLWFAPAEWKECRLGIQLLPLAPISEAIFSNVDFVKELVEWTLPALDREGGVGEGWKGFVYALEGVYDNESALQKIRNLKGFDGGNSLTNLLWWIHSRSDE | ||||||
Glycosylation | 65 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 124 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 160 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 187 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 465 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-208 | beta-sandwich subdomain | ||||
Sequence: VNIQTNTSYIFPQTQSTVLPDPSKFFSSNLLSSPLPTNSFFQNFVLKNGDQQEYIHPYLIKSSNSSLSLSYPSRQASSAVIFQVFNPDLTISAPQGPKQGPPGKHLISSYSDLSVTLDFPSSNLSFFLVRGSPYLTVSVTQPTPLSITTIHSILSFSSNDSNTKYTFQFNNGQTWLLYATSPIKLNHTLSEITSNAFSGIIRIALLP | ||||||
Domain | 2-668 | GH81 | ||||
Sequence: VNIQTNTSYIFPQTQSTVLPDPSKFFSSNLLSSPLPTNSFFQNFVLKNGDQQEYIHPYLIKSSNSSLSLSYPSRQASSAVIFQVFNPDLTISAPQGPKQGPPGKHLISSYSDLSVTLDFPSSNLSFFLVRGSPYLTVSVTQPTPLSITTIHSILSFSSNDSNTKYTFQFNNGQTWLLYATSPIKLNHTLSEITSNAFSGIIRIALLPDSDSKHEAVLDKYSSCYPVSGKAVFREPFCVEYNWEKKDSGDLLLLAHPLHVQLLRNGDNDVKILEDLKYKSIDGDLVGVVGDSWVLKTDPLFVTWHSIKGIKEESHDEIVSALSKDVESLDSSSITTTESYFYGKLIARAARLVLIAEELNYPDVIPKVRNFLKETIEPWLEGTFSGNGFLHDEKWGGIITQKGSTDAGGDFGFGIYNDHHYHLGYFIYGIAVLTKLDPAWGRKYKPQAYSIVQDFLNLDTKLNSNYTRLRCFDPYVLHSWAGGLTEFTDGRNQESTSEAVSAYYSAALMGLAYGDAPLVALGSTLTALEIEGTKMWWHVKEGGTLYEKEFTQENRVMGVLWSNKRDTGLWFAPAEWKECRLGIQLLPLAPISEAIFSNVDFVKELVEWTLPALDREGGVGEGWKGFVYALEGVYDNESALQKIRNLKGFDGGNSLTNLLWWIHSRSDE | ||||||
Region | 209-299 | alpha/beta subdomain | ||||
Sequence: DSDSKHEAVLDKYSSCYPVSGKAVFREPFCVEYNWEKKDSGDLLLLAHPLHVQLLRNGDNDVKILEDLKYKSIDGDLVGVVGDSWVLKTDP | ||||||
Region | 240-443 | Involved in beta-glucan binding | ||||
Sequence: EYNWEKKDSGDLLLLAHPLHVQLLRNGDNDVKILEDLKYKSIDGDLVGVVGDSWVLKTDPLFVTWHSIKGIKEESHDEIVSALSKDVESLDSSSITTTESYFYGKLIARAARLVLIAEELNYPDVIPKVRNFLKETIEPWLEGTFSGNGFLHDEKWGGIITQKGSTDAGGDFGFGIYNDHHYHLGYFIYGIAVLTKLDPAWGRK | ||||||
Region | 309-668 | (alpha/beta)6 barrel subdomain | ||||
Sequence: GIKEESHDEIVSALSKDVESLDSSSITTTESYFYGKLIARAARLVLIAEELNYPDVIPKVRNFLKETIEPWLEGTFSGNGFLHDEKWGGIITQKGSTDAGGDFGFGIYNDHHYHLGYFIYGIAVLTKLDPAWGRKYKPQAYSIVQDFLNLDTKLNSNYTRLRCFDPYVLHSWAGGLTEFTDGRNQESTSEAVSAYYSAALMGLAYGDAPLVALGSTLTALEIEGTKMWWHVKEGGTLYEKEFTQENRVMGVLWSNKRDTGLWFAPAEWKECRLGIQLLPLAPISEAIFSNVDFVKELVEWTLPALDREGGVGEGWKGFVYALEGVYDNESALQKIRNLKGFDGGNSLTNLLWWIHSRSDE | ||||||
Region | 564-566 | May provide specificity for triple-helical beta-glucan | ||||
Sequence: KRD |
Sequence similarities
Belongs to the glycosyl hydrolase 81 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length668
- Mass (Da)74,610
- Last updated2001-12-01 v2
- Checksum0D6992870BFC481E
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 149 | in Ref. 2; CAA71307 | ||||
Sequence: T → A | ||||||
Sequence conflict | 516 | in Ref. 2; CAA71307 | ||||
Sequence: A → V |
Keywords
- Technical term