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P23904 (GUB_PAEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. 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
OrganismPaenibacillus macerans (Bacillus macerans)
Taxonomic identifier44252 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length237 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 – 2323 Potential
Chain24 – 237214Beta-glucanase
PRO_0000011789

Sites

Active site1281Nucleophile By similarity
Active site1321Proton donor By similarity

Amino acid modifications

Disulfide bond55 ↔ 84 Ref.4

Experimental info

Mutagenesis1281E → D, N, A, L, P, R, H, C, S or Y: Loss of activity. Ref.3

Secondary structure

........................................... 237
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23904 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 436EABCDFFC87781

FASTA23726,589
        10         20         30         40         50         60 
MKKKSCFTLV TTFAFSLIFS VSALAGSVFW EPLSYFNRST WEKADGYSNG GVFNCTWRAN 

        70         80         90        100        110        120 
NVNFTNDGKL KLGLTSSAYN KFDCAEYRST NIYGYGLYEV SMKPAKNTGI VSSFFTYTGP 

       130        140        150        160        170        180 
AHGTQWDEID IEFLGKDTTK VQFNYYTNGV GGHEKVISLG FDASKGFHTY AFDWQPGYIK 

       190        200        210        220        230 
WYVDGVLKHT ATANIPSTPG KIMMNLWNGT GVDDWLGSYN GANPLYAEYD WVKYTSN 

« Hide

References

[1]"Structure of the beta-1,3-1,4-glucanase gene of Bacillus macerans: homologies to other beta-glucanases."
Borriss R., Buettner K., Maentsaelae P.
Mol. Gen. Genet. 222:278-283(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Identification of glutamic acid 105 at the active site of Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan 4-glucanohydrolase using epoxide-based inhibitors."
Hoej P.B., Condron R., Traeger J.C., McAuliffe J.C., Stone B.A.
J. Biol. Chem. 267:25059-25066(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[3]Olsen O.
Thesis (1990), University of Aarhus, Denmark
Cited for: MUTAGENESIS OF GLU-128.
[4]"Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase."
Keitel T., Simon O., Borriss R., Heinemann U.
Proc. Natl. Acad. Sci. U.S.A. 90:5287-5291(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]"Crystal and molecular structure at 0.16-nm resolution of the hybrid Bacillus endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase H(A16-M)."
Hahn M., Keitel T., Heinemann U.
Eur. J. Biochem. 232:849-858(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55959 Genomic DNA. Translation: CAA39426.1.
PIRS11927.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJKX-ray1.80A/B107-237[»]
1AJOX-ray2.07A/B37-149[»]
1AXKX-ray2.10A/B82-237[»]
1BYHX-ray2.80A40-237[»]
1CPMX-ray2.00A82-237[»]
1CPNX-ray1.80A82-237[»]
1GLHX-ray2.00A37-237[»]
1MACX-ray2.30A/B26-237[»]
1U0AX-ray1.64A/B/C/D37-237[»]
2AYHX-ray1.60A37-237[»]
ProteinModelPortalP23904.
SMRP23904. Positions 22-237.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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

EvolutionaryTraceP23904.

Entry information

Entry nameGUB_PAEMA
AccessionPrimary (citable) accession number: P23904
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 90 of the entry and version 2 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