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Protein

Beta-glucanase

Gene
N/A
Organism
Paenibacillus macerans (Bacillus macerans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 sitei128 – 1281NucleophilePROSITE-ProRule annotation
Active sitei132 – 1321Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. licheninase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

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
OrganismiPaenibacillus macerans (Bacillus macerans)
Taxonomic identifieri44252 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi128 – 1281E → D, N, A, L, P, R, H, C, S or Y: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 237214Beta-glucanasePRO_0000011789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 841 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
237
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 314Combined sources
Beta strandi38 – 436Combined sources
Beta strandi46 – 483Combined sources
Beta strandi55 – 573Combined sources
Helixi59 – 613Combined sources
Beta strandi62 – 643Combined sources
Beta strandi70 – 789Combined sources
Beta strandi81 – 9111Combined sources
Beta strandi95 – 1039Combined sources
Beta strandi110 – 1189Combined sources
Helixi120 – 1223Combined sources
Beta strandi127 – 1348Combined sources
Helixi135 – 1373Combined sources
Beta strandi140 – 1478Combined sources
Beta strandi155 – 1584Combined sources
Helixi163 – 1653Combined sources
Beta strandi168 – 1758Combined sources
Beta strandi178 – 1836Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi200 – 21112Combined sources
Helixi213 – 2164Combined sources
Beta strandi225 – 23612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP23904.
SMRiP23904. Positions 22-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23904.

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.
IPR013320. ConA-like_dom.
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.

P23904-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKKSCFTLV TTFAFSLIFS VSALAGSVFW EPLSYFNRST WEKADGYSNG
60 70 80 90 100
GVFNCTWRAN NVNFTNDGKL KLGLTSSAYN KFDCAEYRST NIYGYGLYEV
110 120 130 140 150
SMKPAKNTGI VSSFFTYTGP AHGTQWDEID IEFLGKDTTK VQFNYYTNGV
160 170 180 190 200
GGHEKVISLG FDASKGFHTY AFDWQPGYIK WYVDGVLKHT ATANIPSTPG
210 220 230
KIMMNLWNGT GVDDWLGSYN GANPLYAEYD WVKYTSN
Length:237
Mass (Da):26,589
Last modified:June 1, 1994 - v2
Checksum:i436EABCDFFC87781
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55959 Genomic DNA. Translation: CAA39426.1.
PIRiS11927.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55959 Genomic DNA. Translation: CAA39426.1.
PIRiS11927.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP23904.
SMRiP23904. Positions 22-237.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP23904.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008264. Beta_glucanase.
IPR013320. ConA-like_dom.
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]
ProtoNetiSearch...

Publicationsi

  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).

Entry informationi

Entry nameiGUB_PAEMA
AccessioniPrimary (citable) accession number: P23904
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 93 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.