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P27051

- GUB_BACLI

UniProt

P27051 - GUB_BACLI

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Protein

Beta-glucanase

Gene
bg1
Organism
Bacillus licheniformis
Status
Reviewed - Annotation score: 5 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 sitei134 – 1341Nucleophile
Active sitei138 – 1381Proton donor

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

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 – 2727 Reviewed predictionAdd
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.

Miscellaneous databases

EvolutionaryTraceiP27051.

Family & Domainsi

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2321S → Y1 Publication

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 16, 2013
This is version 80 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

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