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Protein

Glucan endo-1,3-beta-glucosidase GII

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei259 – 2591Nucleophile
Active sitei316 – 3161Proton donor

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Plant defense

Enzyme and pathway databases

SABIO-RKP15737.

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

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

Organism-specific databases

GrameneiP15737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28282 PublicationsAdd
BLAST
Chaini29 – 334306Glucan endo-1,3-beta-glucosidase GIIPRO_0000011848Add
BLAST

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Beta strandi37 – 393Combined sources
Helixi43 – 5311Combined sources
Beta strandi57 – 626Combined sources
Helixi65 – 706Combined sources
Turni71 – 733Combined sources
Beta strandi77 – 815Combined sources
Helixi84 – 863Combined sources
Helixi87 – 926Combined sources
Helixi94 – 10411Combined sources
Turni105 – 1117Combined sources
Beta strandi112 – 12211Combined sources
Helixi125 – 1306Combined sources
Helixi131 – 14515Combined sources
Beta strandi150 – 1578Combined sources
Helixi158 – 1603Combined sources
Helixi167 – 1693Combined sources
Beta strandi171 – 1744Combined sources
Helixi176 – 18712Combined sources
Beta strandi191 – 1944Combined sources
Helixi197 – 2037Combined sources
Turni205 – 2073Combined sources
Helixi210 – 2145Combined sources
Turni224 – 2263Combined sources
Helixi233 – 24816Combined sources
Beta strandi255 – 2606Combined sources
Beta strandi264 – 2674Combined sources
Helixi272 – 28312Combined sources
Helixi286 – 2883Combined sources
Beta strandi299 – 3024Combined sources
Helixi314 – 3185Combined sources
Beta strandi328 – 3303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GHSX-ray2.30A/B29-334[»]
ProteinModelPortaliP15737.
SMRiP15737. Positions 29-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15737.

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.

P15737-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKDVASMF AAALFIGAFA AVPTSVQSIG VCYGVIGNNL PSRSDVVQLY
60 70 80 90 100
RSKGINGMRI YFADGQALSA LRNSGIGLIL DIGNDQLANI AASTSNAASW
110 120 130 140 150
VQNNVRPYYP AVNIKYIAAG NEVQGGATQS ILPAMRNLNA ALSAAGLGAI
160 170 180 190 200
KVSTSIRFDE VANSFPPSAG VFKNAYMTDV ARLLASTGAP LLANVYPYFA
210 220 230 240 250
YRDNPGSISL NYATFQPGTT VRDQNNGLTY TSLFDAMVDA VYAALEKAGA
260 270 280 290 300
PAVKVVVSES GWPSAGGFAA SAGNARTYNQ GLINHVGGGT PKKREALETY
310 320 330
IFAMFNENQK TGDATERSFG LFNPDKSPAY NIQF
Length:334
Mass (Da):35,194
Last modified:April 1, 1990 - v1
Checksum:i552D66A29A08C703
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121A → V in AAA32939 (PubMed:1899089).Curated
Sequence conflicti71 – 711L → V in AAA32939 (PubMed:1899089).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62907 mRNA. Translation: AAA32939.1.
X16274 mRNA. Translation: CAA34350.1.
M23548 mRNA. Translation: AAA32958.1.
PIRiS05510.
UniGeneiHv.18110.
Hv.25599.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62907 mRNA. Translation: AAA32939.1.
X16274 mRNA. Translation: CAA34350.1.
M23548 mRNA. Translation: AAA32958.1.
PIRiS05510.
UniGeneiHv.18110.
Hv.25599.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GHSX-ray2.30A/B29-334[»]
ProteinModelPortaliP15737.
SMRiP15737. Positions 29-334.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiP15737.

Enzyme and pathway databases

SABIO-RKP15737.

Miscellaneous databases

EvolutionaryTraceiP15737.

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. "Purification of (1-->3)-beta-glucan endohydrolase isoenzyme II from germinated barley and determination of its primary structure from a cDNA clone."
    Hoej P.B., Hartman D.J., Morrice N.A., Doan D.N.P., Fincher G.B.
    Plant Mol. Biol. 13:31-42(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-68.
    Strain: cv. Clipper.
  2. "Biochemical and molecular characterization of three barley seed proteins with antifungal properties."
    Leah R., Tommerup H., Svendsen I., Mundy J.
    J. Biol. Chem. 266:1564-1573(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Piggy.
  3. Jutidamrongphan W., Mackinnon G., Manners J., Simpson R.S., Scott K.J.
    Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 258-332.
    Tissue: Leaf.
  4. "Purification and amino acid sequence determination of an endo-1,3-beta-glucanase from barley."
    Ballance G.M., Svendsen I.
    Carlsberg Res. Commun. 53:411-419(1988)
    Cited for: PROTEIN SEQUENCE OF 29-334.
  5. "Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities."
    Varghese J.N., Garrett T.P.J., Colman P.M., Chen L., Hoej P.B., Fincher G.B.
    Proc. Natl. Acad. Sci. U.S.A. 91:2785-2789(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiE13B_HORVU
AccessioniPrimary (citable) accession number: P15737
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 24, 2015
This is version 95 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

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.