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P12257

- GUB2_HORVU

UniProt

P12257 - GUB2_HORVU

Protein

Lichenase-2

Gene
N/A
Organism
Hordeum vulgare (Barley)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    Functioni

    Functions in plant cell wall hydrolysis during mobilization of the endosperm in germinating grain or during the growth of vegetative tissues.

    Catalytic activityi

    Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei238 – 2381Nucleophile
    Active sitei294 – 2941Proton donor

    GO - Molecular functioni

    1. licheninase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    UniPathwayiUPA00350.

    Protein family/group databases

    CAZyiGH17. Glycoside Hydrolase Family 17.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lichenase-2 (EC:3.2.1.73)
    Alternative name(s):
    (1->3,1->4)-beta-glucanase isoenzyme EII
    Endo-beta-1,3-1,4 glucanase II
    Lichenase II
    OrganismiHordeum vulgare (Barley)
    Taxonomic identifieri4513 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

    Organism-specific databases

    GrameneiP12257.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei‹1 – 6›61 Publication
    Chaini7 – 312306Lichenase-2PRO_0000011897Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi196 – 1961N-linked (GlcNAc...)

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Gene expression databases

    GenevestigatoriP12257.

    Structurei

    Secondary structure

    1
    312
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103
    Helixi21 – 3111
    Beta strandi35 – 406
    Helixi43 – 497
    Beta strandi55 – 606
    Helixi62 – 643
    Helixi65 – 706
    Helixi72 – 8211
    Turni83 – 853
    Beta strandi89 – 9911
    Helixi102 – 1076
    Helixi108 – 12114
    Beta strandi127 – 1348
    Helixi135 – 1373
    Beta strandi138 – 1403
    Helixi144 – 1463
    Helixi151 – 16717
    Beta strandi171 – 1744
    Helixi177 – 1837
    Turni185 – 1873
    Helixi190 – 1945
    Beta strandi201 – 2044
    Beta strandi207 – 2093
    Helixi212 – 22514
    Turni226 – 2283
    Beta strandi234 – 2385
    Beta strandi243 – 2464
    Helixi251 – 26414
    Turni265 – 2673
    Beta strandi270 – 2745
    Beta strandi278 – 2814
    Helixi293 – 2953
    Beta strandi306 – 3083

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AQ0X-ray2.00A/B7-312[»]
    1GHRX-ray2.20A7-312[»]
    ProteinModelPortaliP12257.
    SMRiP12257. Positions 7-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12257.

    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: Fragment.

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

    P12257-1 [UniParc]FASTAAdd to Basket

    « Hide

    PPSVESIGVC YGMSANNLPA ASTVVSMFKF NGIKSMRLYA PNQAALQAVG    50
    GTGINVVVGA PNDVLSNLAA SPAAAASWVK SNIQAYPKVS FRYVCVGNEV 100
    AGGATRNLVP AMKNVHGALV AAGLGHIKVT TSVSQAILGV FSPPSAGSFT 150
    GEAAAFMGPV VQFLARTNAP LMANIYPYLA WAYNPSAMDM GYALFNASGT 200
    VVRDGAYGYQ NLFDTTVDAF YTAMGKHGGS SVKLVVSESG WPSGGGTAAT 250
    PANARFYNQH LINHVGRGTP RHPGAIETYI FAMFNENQKD SGVEQNWGLF 300
    YPNMQHVYPI NF 312
    Length:312
    Mass (Da):32,774
    Last modified:October 1, 1989 - v1
    Checksum:i7D18C2A6DF522E17
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13237 mRNA. Translation: AAA32962.1.
    PIRiA25455.
    UniGeneiHv.24806.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13237 mRNA. Translation: AAA32962.1 .
    PIRi A25455.
    UniGenei Hv.24806.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AQ0 X-ray 2.00 A/B 7-312 [» ]
    1GHR X-ray 2.20 A 7-312 [» ]
    ProteinModelPortali P12257.
    SMRi P12257. Positions 7-312.
    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 P12257.

    Enzyme and pathway databases

    UniPathwayi UPA00350 .

    Miscellaneous databases

    EvolutionaryTracei P12257.

    Gene expression databases

    Genevestigatori P12257.

    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. "Primary structure of the (1-3,1-4)-beta-D-glucan 4-glucohydrolase from barley aleurone."
      Fincher G.B., Lock P.A., Morgan M.M., Lingelbach K., Wettenhall R.E.H., Mercer J.F.B., Brandt A., Thomsen K.K.
      Proc. Natl. Acad. Sci. U.S.A. 83:2081-2085(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-291, PROTEIN SEQUENCE OF 292-312.
      Strain: cv. Himalaya.
    2. "Amino acid sequence homology in two 1,3;1,4-beta-glucan endohydrolases from germinating barley (Hordeum vulgare)."
      Woodward J.R., Morgan F.J., Fincher G.B.
      FEBS Lett. 138:198-200(1982)
      Cited for: PROTEIN SEQUENCE OF 7-46.
      Strain: cv. Clipper.
      Tissue: Seed.
    3. "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 (2.2 ANGSTROMS).
    4. "Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1,3-1,4-beta-glucanase."
      Mueller J.J., Thomsen K.K., Heinemann U.
      J. Biol. Chem. 273:3438-3446(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiGUB2_HORVU
    AccessioniPrimary (citable) accession number: P12257
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 92 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3