Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P27051 (GUB_BACLI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:bg1
OrganismBacillus licheniformis
Taxonomic identifier1402 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Miscellaneous

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

Sequence similarities

Belongs to the glycosyl hydrolase 16 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionlicheninase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 243216Beta-glucanase
PRO_0000011788

Sites

Active site1341Nucleophile
Active site1381Proton donor

Amino acid modifications

Disulfide bond61 ↔ 90 Ref.5

Experimental info

Mutagenesis511D → N: 30% of wild-type activity.
Mutagenesis891D → N: 85% of wild-type activity.
Mutagenesis921E → Q: 3% of wild-type activity.
Mutagenesis1051E → Q: 50% of wild-type activity.
Mutagenesis1331D → N: 15% of wild-type activity.
Mutagenesis1341E → Q: 0.2% of wild-type activity.
Mutagenesis1361D → N: 0.5% of wild-type activity.
Mutagenesis1381E → Q: Complete loss of activity.
Mutagenesis1431D → N: 65% of wild-type activity.
Mutagenesis1601E → Q: 15% of wild-type activity.
Mutagenesis1681D → N: 60% of wild-type activity.
Mutagenesis1791D → N: 80% of wild-type activity.
Mutagenesis1901D → N: 70% of wild-type activity.
Mutagenesis2191D → N: No change in activity.
Sequence conflict2321S → Y Ref.5

Secondary structure

......................................... 243
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27051 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 651188D9AAD609A5

FASTA24327,435
        10         20         30         40         50         60 
MSYRVKRMLM LLVTGLFLSL STFAASASAQ TGGSFYEPFN NYNTGLWQKA DGYSNGNMFN 

        70         80         90        100        110        120 
CTWRANNVSM TSLGEMRLSL TSPSYNKFDC GENRSVQTYG YGLYEVNMKP AKNVGIVSSF 

       130        140        150        160        170        180 
FTYTGPTDGT PWDEIDIEFL GKDTTKVQFN YYTNGVGNHE KIVNLGFDAA NSYHTYAFDW 

       190        200        210        220        230        240 
QPNSIKWYVD GQLKHTATTQ IPQTPGKIMM NLWNGAGVDE WLGSYNGVTP LSRSLHWVRY 


TKR 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57279 Genomic DNA. Translation: CAA40547.1.
PIRS15388.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GBGX-ray1.80A30-243[»]
3D6EX-ray2.40A/B30-243[»]
ProteinModelPortalP27051.
SMRP27051. Positions 30-243.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP27051.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008264. Beta_glucanase.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view]
PfamPF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PRINTSPR00737. GLHYDRLASE16.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP27051.

Entry information

Entry nameGUB_BACLI
AccessionPrimary (citable) accession number: P27051
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 16, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries