Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glucan endo-1,3-beta-glucosidase, basic isoform 3

Gene

GLUB3

Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Is thought to be an important plant defense-related product against fungal pathogens.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei230 – 2301NucleophileBy similarity
Active sitei286 – 2861Proton donorBy similarity

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. defense response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Plant defense

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan endo-1,3-beta-glucosidase, basic isoform 3 (EC:3.2.1.39)
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name:
(1->3)-beta-glucanase
Beta-1,3-endoglucanase
Gene namesi
Name:GLUB3
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115: Unplaced

Subcellular locationi

Vacuole By similarity

GO - Cellular componenti

  1. vacuole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Protein family/group databases

Allergomei2551. Sola t Glucanase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 305›305Glucan endo-1,3-beta-glucosidase, basic isoform 3PRO_0000011864Add
BLAST
Propeptidei306 – 32823Removed in mature formBy similarityPRO_0000011865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Expressioni

Developmental stagei

Highest levels in old segments of leaves, stems and roots.

Inductioni

In response to infection, elicitor, ethylene, wounding.

Structurei

3D structure databases

ProteinModelPortaliP52402.
SMRiP52402. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Phylogenomic databases

InParanoidiP52402.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52402-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NNLPSHSEVI QLYKSRNIGR LRLYDPNHGA LNALRGSNIE VILGLPNVDV
60 70 80 90 100
KHIASGMEHA RWWVQKNVKD FWPDVKIKYI AVGNEISPVT GTSSLTSFQV
110 120 130 140 150
PALVNIYKAI GEAGLGNDIK VSTSVDMTLI GNSYPPSQGS FRNDVRWFTD
160 170 180 190 200
PIVGFLRDTR APLLVNIYPY FSYSGNPGQI SLPYALFTAP NVVVQDGSRQ
210 220 230 240 250
YRNLFDAMLD SVYAAMERTG GGSVGIVVSE SGWPSAGAFG ATQDNAATYL
260 270 280 290 300
RNLIQHAKEG SPRKPGPIET YIFAMFDENN KNPELEKHFG LFSPNKQPKY
310 320
NLNFGVSERV WDISAETNST TSSLISEM
Length:328
Mass (Da):36,182
Last modified:October 1, 1996 - v1
Checksum:iF2F9266304B89454
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01902 mRNA. Translation: AAA19111.1.
PIRiS65023.
UniGeneiStu.19464.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01902 mRNA. Translation: AAA19111.1.
PIRiS65023.
UniGeneiStu.19464.

3D structure databases

ProteinModelPortaliP52402.
SMRiP52402. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei2551. Sola t Glucanase.
CAZyiGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiP52402.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure and expression of mRNAs encoding basic chitinase and 1,3-beta-glucanase in potato."
    Beerhues L., Kombrink E.
    Plant Mol. Biol. 24:353-367(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Datura.
    Tissue: Leaf.

Entry informationi

Entry nameiE133_SOLTU
AccessioniPrimary (citable) accession number: P52402
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.