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Protein

Glucan endo-1,3-beta-glucosidase, acidic isoform PR-O

Gene

PR0

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Implicated in the defense of plants against 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 sitei81 – 811NucleophileBy similarity
Active sitei141 – 1411Proton 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, acidic isoform PR-O (EC:3.2.1.39)
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name:
(1->3)-beta-glucanase
Beta-1,3-endoglucanase
PR-37
Gene namesi
Name:PR0
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 160›160Glucan endo-1,3-beta-glucosidase, acidic isoform PR-OPRO_0000205278Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

PRIDEiP52397.

Expressioni

Inductioni

Not found in healthy tissues, but accumulates to high levels in the extracellular compartment of leaves in response to pathogen infection or treatment with salicylic acid.

Structurei

3D structure databases

ProteinModelPortaliP52397.
SMRiP52397. Positions 2-159.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

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.

P52397-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
NSFINPIIQF LARNNLPLLA NVYPYFGHIY NTADVPLSYA LFTQQEANPA
60 70 80 90 100
GYQNLFDALL DSMYFAVEKA GGPNVEIIVS ESGWPSEGNS AATIENAQTY
110 120 130 140 150
YRNLIDHVKR GAGTPKKPGK TIETYLFAMF DENDKKGEIT EKHFGLFSPD
160
QRAKYQLNFN
Length:160
Mass (Da):17,980
Last modified:October 1, 1996 - v1
Checksum:i98C270F390764B7F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti128 – 1281A → N AA sequence (PubMed:16594025)Curated
Sequence conflicti135 – 1351K → Q AA sequence (PubMed:16594025)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60461 mRNA. Translation: AAA34102.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60461 mRNA. Translation: AAA34102.1.

3D structure databases

ProteinModelPortaliP52397.
SMRiP52397. Positions 2-159.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Proteomic databases

PRIDEiP52397.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. "Differential regulation of beta-1,3-glucanase messenger RNAs in response to pathogen infection."
    Ward E.R., Payne G.B., Moyer M.B., Williams S.C., Dincher S.S., Sharkey K.C., Beck J.J., Taylor H.T., Ahl-Goy P., Meins F., Ryals J.A.
    Plant Physiol. 96:390-397(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Xanthi NC.
    Tissue: Leaf.
  2. "Characterization of vacuolar and extracellular beta(1,3)-glucanases of tobacco: evidence for a strictly compartmentalized plant defense system."
    van den Bulcke M., Bauw G., Castresana C., van Montagu M., Vandekerckhove J.
    Proc. Natl. Acad. Sci. U.S.A. 86:2673-2677(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 70-93; 126-136; 143-152 AND 155-160.

Entry informationi

Entry nameiE13J_TOBAC
AccessioniPrimary (citable) accession number: P52397
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 73 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

Direct protein sequencing

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.