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P15737

- E13B_HORVU

UniProt

P15737 - E13B_HORVU

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Protein
Glucan endo-1,3-beta-glucosidase GII
Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed - 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

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

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

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Organism-specific databases

GrameneiP15737.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28282 Publications
Add
BLAST
Chaini29 – 334306Glucan endo-1,3-beta-glucosidase GII
PRO_0000011848Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP15737.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GHSX-ray2.30A/B29-334[»]
ProteinModelPortaliP15737.
SMRiP15737. Positions 29-334.

Miscellaneous databases

EvolutionaryTraceiP15737.

Family & Domainsi

Sequence similaritiesi

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

MARKDVASMF AAALFIGAFA AVPTSVQSIG VCYGVIGNNL PSRSDVVQLY    50
RSKGINGMRI YFADGQALSA LRNSGIGLIL DIGNDQLANI AASTSNAASW 100
VQNNVRPYYP AVNIKYIAAG NEVQGGATQS ILPAMRNLNA ALSAAGLGAI 150
KVSTSIRFDE VANSFPPSAG VFKNAYMTDV ARLLASTGAP LLANVYPYFA 200
YRDNPGSISL NYATFQPGTT VRDQNNGLTY TSLFDAMVDA VYAALEKAGA 250
PAVKVVVSES GWPSAGGFAA SAGNARTYNQ GLINHVGGGT PKKREALETY 300
IFAMFNENQK TGDATERSFG LFNPDKSPAY NIQF 334
Length:334
Mass (Da):35,194
Last modified:April 1, 1990 - v1
Checksum:i552D66A29A08C703
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121A → V in AAA32939. 1 Publication
Sequence conflicti71 – 711L → V in AAA32939. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M62907 mRNA. Translation: AAA32939.1 .
X16274 mRNA. Translation: CAA34350.1 .
M23548 mRNA. Translation: AAA32958.1 .
PIRi S05510.
UniGenei Hv.18110.
Hv.25599.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GHS X-ray 2.30 A/B 29-334 [» ]
ProteinModelPortali P15737.
SMRi P15737. Positions 29-334.
ModBasei Search...

Protein family/group databases

CAZyi GH17. Glycoside Hydrolase Family 17.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei P15737.

Enzyme and pathway databases

SABIO-RK P15737.

Miscellaneous databases

EvolutionaryTracei P15737.

Gene expression databases

Genevestigatori P15737.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00332. Glyco_hydro_17. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 16, 2013
This is version 90 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

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