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P23904

- GUB_PAEMA

UniProt

P23904 - GUB_PAEMA

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Protein
Beta-glucanase
Gene
N/A
Organism
Paenibacillus macerans (Bacillus macerans)
Status
Reviewed - 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 – 1281Nucleophile By similarity
Active sitei132 – 1321Proton donor By similarity

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 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 237214Beta-glucanase
PRO_0000011789Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP23904.

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.

P23904-1 [UniParc]FASTAAdd to Basket

« Hide

MKKKSCFTLV TTFAFSLIFS VSALAGSVFW EPLSYFNRST WEKADGYSNG    50
GVFNCTWRAN NVNFTNDGKL KLGLTSSAYN KFDCAEYRST NIYGYGLYEV 100
SMKPAKNTGI VSSFFTYTGP AHGTQWDEID IEFLGKDTTK VQFNYYTNGV 150
GGHEKVISLG FDASKGFHTY AFDWQPGYIK WYVDGVLKHT ATANIPSTPG 200
KIMMNLWNGT GVDDWLGSYN GANPLYAEYD WVKYTSN 237
Length:237
Mass (Da):26,589
Last modified:June 1, 1994 - v2
Checksum:i436EABCDFFC87781
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55959 Genomic DNA. Translation: CAA39426.1.
PIRiS11927.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55959 Genomic DNA. Translation: CAA39426.1 .
PIRi S11927.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AJK X-ray 1.80 A/B 107-237 [» ]
1AJO X-ray 2.07 A/B 37-149 [» ]
1AXK X-ray 2.10 A/B 82-237 [» ]
1BYH X-ray 2.80 A 40-237 [» ]
1CPM X-ray 2.00 A 82-237 [» ]
1CPN X-ray 1.80 A 82-237 [» ]
1GLH X-ray 2.00 A 37-237 [» ]
1MAC X-ray 2.30 A/B 26-237 [» ]
1U0A X-ray 1.64 A/B/C/D 37-237 [» ]
2AYH X-ray 1.60 A 37-237 [» ]
ProteinModelPortali P23904.
SMRi P23904. Positions 22-237.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P23904.

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. "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: July 9, 2014
This is version 90 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

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