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P15737

- E13B_HORVU

UniProt

P15737 - E13B_HORVU

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
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. defense response Source: UniProtKB-KW

    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 PublicationsAdd
    BLAST
    Chaini29 – 334306Glucan endo-1,3-beta-glucosidase GIIPRO_0000011848Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP15737.

    Structurei

    Secondary structure

    1
    334
    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.
    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

    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

    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:
    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...
    MobiDBi 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 1, 2014
    This is version 91 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