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Protein

Glucan endo-1,3-beta-glucosidase GIII

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May provide a degree of protection against microbial invasion of germinated barley grain through its ability to degrade fungal cell wall polysaccharides.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei255NucleophileBy similarity1
Active sitei312Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Plant defense

Enzyme and pathway databases

BRENDAi3.2.1.39. 2687.
SABIO-RKQ02126.

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan endo-1,3-beta-glucosidase GIII (EC:3.2.1.39)
Alternative name(s):
(1->3)-beta-glucan endohydrolase GIII
(1->3)-beta-glucanase isoenzyme GIII
Beta-1,3-endoglucanase GIII
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
ChainiPRO_000001184926 – 330Glucan endo-1,3-beta-glucosidase GIIIAdd BLAST305

Expressioni

Developmental stagei

Accumulates in developing leaves.

Structurei

3D structure databases

ProteinModelPortaliQ02126.
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.

Q02126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKGVDVAV ALVLVALAAF PAVHSIGVCN GVLGNNLPAP SDVVTLYRSK
60 70 80 90 100
RIDAMRIYEP ESKVLTALSG TGIAVLMDVG PALPSLASSP SAAAAWVKAN
110 120 130 140 150
VSSFPGVSFR YIAVRNEVMD SAGQSTILPA MRNVQRALAA AGSPIKVSTS
160 170 180 190 200
VRFDVFNNTS PPSNGVLADK SGFLRPILNF LARPARPLLA NVYPYFAYKG
210 220 230 240 250
NPRDIQLTFA TFVPGSTTVN DNGLTYTNLF DAMVDSIYAA LEKAGTPGVK
260 270 280 290 300
VVISESGWPS DQGFGATAQN ARAYNQGLIN HVGNGSPKKA GALESYIFAM
310 320 330
FNENLKDGDE LEKNFGLFKP NMSPAYAITF
Length:330
Mass (Da):34,887
Last modified:February 1, 1994 - v1
Checksum:iB8A262CF345A79E7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti169D → S (PubMed:1398132).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67099 Genomic DNA. Translation: CAA47473.1.
PIRiS29311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67099 Genomic DNA. Translation: CAA47473.1.
PIRiS29311.

3D structure databases

ProteinModelPortaliQ02126.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.39. 2687.
SABIO-RKQ02126.

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...

Entry informationi

Entry nameiE13C_HORVU
AccessioniPrimary (citable) accession number: Q02126
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 5, 2016
This is version 75 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

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 one 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.