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Protein

Glucan endo-1,3-beta-glucosidase, acidic isoform PR-Q'

Gene
N/A
Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei262 – 2621NucleophileBy similarity
Active sitei320 – 3201Proton 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-Q' (EC:3.2.1.39)
Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name:
(1->3)-beta-glucanase
Beta-1,3-endoglucanase
PR-35
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Apoplast, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 339315Glucan endo-1,3-beta-glucosidase, acidic isoform PR-Q'PRO_0000011878Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Pyrrolidone carboxylic acidCurated

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Pyrrolidone carboxylic acid

Expressioni

Inductioni

Accumulates following infection.

Structurei

3D structure databases

ProteinModelPortaliP36401.
SMRiP36401. Positions 26-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

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: Complete.

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

P36401-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHLIVTLLL LSVLTLATLD FTGAQAGVCY GRQGNGLPSP ADVVSLCNRN
60 70 80 90 100
NIRRMRIYDP DQPTLEALRG SNIELMLGVP NPDLENVAAS QANADTWVQN
110 120 130 140 150
NVRNYGNVKF RYIAVGNEVS PLNENSKYVP VLLNAMRNIQ TAISGAGLGN
160 170 180 190 200
QIKVSTAIET GLTTDTSPPS NGRFKDDVRQ FIEPIINFLV TNRAPLLVNL
210 220 230 240 250
YPYFAIANNA DIKLEYALFT SSEVVVNDNG RGYRNLFDAI LDATYSALEK
260 270 280 290 300
ASGSSLEIVV SESGWPSAGA GQLTSIDNAR TYNNNLISHV KGGSPKRPSG
310 320 330
PIETYVFALF DEDQKDPEIE KHFGLFSANM QPKYQISFN
Length:339
Mass (Da):36,995
Last modified:June 1, 1994 - v1
Checksum:iFDFA0D4F7300235E
GO

Sequence cautioni

The sequence CAA38324.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti297 – 2971R → A AA sequence (PubMed:16594025).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54456 mRNA. Translation: CAA38324.1. Different initiation.
PIRiS12402.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54456 mRNA. Translation: CAA38324.1. Different initiation.
PIRiS12402.

3D structure databases

ProteinModelPortaliP36401.
SMRiP36401. Positions 26-338.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

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. "Evidence for a third structural class of beta-1,3-glucanase in tobacco."
    Payne G., Ward E., Gaffney T., Ahl Goy P., Moyer M., Harper A., Meins F. Jr., Ryals J.
    Plant Mol. Biol. 15:797-808(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Xanthi.
  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(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 57-69; 112-126; 281-291; 297-321 AND 333-339.

Entry informationi

Entry nameiE13H_TOBAC
AccessioniPrimary (citable) accession number: P36401
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 7, 2015
This is version 82 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.