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P27051

- GUB_BACLI

UniProt

P27051 - GUB_BACLI

Protein

Beta-glucanase

Gene

bg1

Organism
Bacillus licheniformis
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei134 – 1341Nucleophile
    Active sitei138 – 1381Proton 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

    SABIO-RKP27051.

    Protein family/group databases

    CAZyiGH16. Glycoside Hydrolase Family 16.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucanase (EC:3.2.1.73)
    Alternative name(s):
    1,3-1,4-beta-D-glucan 4-glucanohydrolase
    Endo-beta-1,3-1,4 glucanase
    Lichenase
    Gene namesi
    Name:bg1
    OrganismiBacillus licheniformis
    Taxonomic identifieri1402 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511D → N: 30% of wild-type activity.
    Mutagenesisi89 – 891D → N: 85% of wild-type activity.
    Mutagenesisi92 – 921E → Q: 3% of wild-type activity.
    Mutagenesisi105 – 1051E → Q: 50% of wild-type activity.
    Mutagenesisi133 – 1331D → N: 15% of wild-type activity.
    Mutagenesisi134 – 1341E → Q: 0.2% of wild-type activity.
    Mutagenesisi136 – 1361D → N: 0.5% of wild-type activity.
    Mutagenesisi138 – 1381E → Q: Complete loss of activity.
    Mutagenesisi143 – 1431D → N: 65% of wild-type activity.
    Mutagenesisi160 – 1601E → Q: 15% of wild-type activity.
    Mutagenesisi168 – 1681D → N: 60% of wild-type activity.
    Mutagenesisi179 – 1791D → N: 80% of wild-type activity.
    Mutagenesisi190 – 1901D → N: 70% of wild-type activity.
    Mutagenesisi219 – 2191D → N: No change in activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 243216Beta-glucanasePRO_0000011788Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi61 ↔ 901 Publication

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    243
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 373
    Turni44 – 463
    Beta strandi47 – 493
    Beta strandi61 – 633
    Helixi65 – 673
    Beta strandi68 – 703
    Beta strandi76 – 849
    Beta strandi87 – 9711
    Beta strandi101 – 1099
    Beta strandi116 – 1249
    Helixi126 – 1283
    Beta strandi133 – 1408
    Beta strandi146 – 1538
    Beta strandi161 – 1644
    Turni169 – 1713
    Beta strandi174 – 1818
    Beta strandi184 – 1896
    Beta strandi192 – 1976
    Beta strandi206 – 21712
    Helixi219 – 2224
    Beta strandi231 – 24212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GBGX-ray1.80A30-243[»]
    3D6EX-ray2.40A/B30-243[»]
    ProteinModelPortaliP27051.
    SMRiP27051. Positions 30-243.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27051.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 16 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008264. Beta_glucanase.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000757. Glyco_hydro_16.
    IPR008263. Glycoside_hydrolase_16_AS.
    [Graphical view]
    PfamiPF00722. Glyco_hydro_16. 1 hit.
    [Graphical view]
    PRINTSiPR00737. GLHYDRLASE16.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS01034. GLYCOSYL_HYDROL_F16. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P27051-1 [UniParc]FASTAAdd to Basket

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    MSYRVKRMLM LLVTGLFLSL STFAASASAQ TGGSFYEPFN NYNTGLWQKA    50
    DGYSNGNMFN CTWRANNVSM TSLGEMRLSL TSPSYNKFDC GENRSVQTYG 100
    YGLYEVNMKP AKNVGIVSSF FTYTGPTDGT PWDEIDIEFL GKDTTKVQFN 150
    YYTNGVGNHE KIVNLGFDAA NSYHTYAFDW QPNSIKWYVD GQLKHTATTQ 200
    IPQTPGKIMM NLWNGAGVDE WLGSYNGVTP LSRSLHWVRY TKR 243
    Length:243
    Mass (Da):27,435
    Last modified:August 1, 1992 - v1
    Checksum:i651188D9AAD609A5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti232 – 2321S → Y(PubMed:7589539)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57279 Genomic DNA. Translation: CAA40547.1.
    PIRiS15388.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57279 Genomic DNA. Translation: CAA40547.1 .
    PIRi S15388.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GBG X-ray 1.80 A 30-243 [» ]
    3D6E X-ray 2.40 A/B 30-243 [» ]
    ProteinModelPortali P27051.
    SMRi P27051. Positions 30-243.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH16. Glycoside Hydrolase Family 16.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P27051.

    Miscellaneous databases

    EvolutionaryTracei P27051.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008264. Beta_glucanase.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000757. Glyco_hydro_16.
    IPR008263. Glycoside_hydrolase_16_AS.
    [Graphical view ]
    Pfami PF00722. Glyco_hydro_16. 1 hit.
    [Graphical view ]
    PRINTSi PR00737. GLHYDRLASE16.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, expression and nucleotide sequence of the endo-beta-1,3-1,4-D-glucanase gene from Bacillus licheniformis. Predictive structural analyses of the encoded polypeptide."
      Lloberas J., Perez-Pons J.A., Querol E.
      Eur. J. Biochem. 197:337-343(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Querol E.
      Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Essential catalytic role of Glu134 in endo-beta-1,3-1,4-D-glucan 4-glucanohydrolase from B. licheniformis as determined by site-directed mutagenesis."
      Planas A., Juncosa M., Lloberas J., Querol E.
      FEBS Lett. 308:141-145(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    4. "Identification of active site carboxylic residues in Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase by site-directed mutagenesis."
      Juncosa M., Pons J., Dot T., Querol E., Planas A.
      J. Biol. Chem. 269:14530-14535(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    5. "Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8-A resolution."
      Hahn M., Pons J., Planas A., Querol E., Heinemann U.
      FEBS Lett. 374:221-224(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), DISULFIDE BOND.

    Entry informationi

    Entry nameiGUB_BACLI
    AccessioniPrimary (citable) accession number: P27051
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Beta-glucanases of Bacillus have a substrate range similar to lichenase of germinating barley.

    Keywords - Technical termi

    3D-structure

    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