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

P29019 (GUN_BACSZ) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Endoglucanase

EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Endo-K
OrganismBacillus sp. (strain KSM-330)
Taxonomic identifier72575 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Post-translational modification

The N- and the C-terminus may be subjected to proteolysis.

Miscellaneous

One Trp residue has been proved to be involved in the mechanism of action of endo-K.

Sequence similarities

Belongs to the glycosyl hydrolase 8 (cellulase D) family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.2. Active from pH 4.5 to 6.5.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncellulase 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
Propeptide28 – 5528 Potential
PRO_0000007931
Chain56 – 463408Endoglucanase
PRO_0000007932

Sites

Active site1301Proton donor By similarity
Active site1911Nucleophile Potential

Sequences

Sequence LengthMass (Da)Tools
P29019 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 407FA54F5236C59E

FASTA46351,883
        10         20         30         40         50         60 
MVEKRKIFTV LCACGIGFTS YTSCISAAAI DNDTLINNGH KINSSIITNS SQVSAVAKEM 

        70         80         90        100        110        120 
KPFPQQVNYS GILKPNHVSQ ESLNNAVKNY YNDWKKKYLK NDLSSLPGGY YVKGEITGNP 

       130        140        150        160        170        180 
DGFRPLGTSE GQGYGMIITV LMAGHDSNAQ TIYDGLFKTA RAFKSSINPN LMGWVVADDK 

       190        200        210        220        230        240 
KAQGHFDSAT DGDLDIAYSL LLAHKQWGSS GKINYLKEAQ NMITKGIKAS NVTKNNGLNL 

       250        260        270        280        290        300 
GDWGDKSTFD TRPSDWMMSH LRAFYEFTGD KTWLNVIDNL YNTYTNFTNK YSPKTGLISD 

       310        320        330        340        350        360 
FVVKNPPQPA PKDFLDESKY TDSYYYNASR VPLRIVMDYA MYGEKRGKVI SDKVATWIKS 

       370        380        390        400        410        420 
KTKGNPSKIV DGYKLDGTNI GDYPTAVYVS PFIAAGTTNS KNQEWVNSGW DWMKNKKESY 

       430        440        450        460 
FSDSYNLLTM LFLTGNWWKP IPDEKKIQSP INLEVQSELK EQD 

« Hide

References

[1]"Molecular cloning and nucleotide sequence of the gene encoding an endo-1,4-beta-glucanase from Bacillus sp. KSM-330."
Ozaki K., Sumitomo N., Ito S.
J. Gen. Microbiol. 137:2299-2305(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Purification and properties of an acid endo-1,4-beta-glucanase from Bacillus sp. KSM-330."
Ozaki K., Ito S.
J. Gen. Microbiol. 137:41-48(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 56-75, CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M68872 Genomic DNA. Translation: AAA22409.1.
PIRA44808.

3D structure databases

ProteinModelPortalP29019.
SMRP29019. Positions 57-442.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH8. Glycoside Hydrolase Family 8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.50.10.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR002037. Glyco_hydro_8.
IPR019834. Glyco_hydro_8_CS.
[Graphical view]
PfamPF01270. Glyco_hydro_8. 1 hit.
[Graphical view]
PRINTSPR00735. GLHYDRLASE8.
SUPFAMSSF48208. SSF48208. 1 hit.
PROSITEPS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN_BACSZ
AccessionPrimary (citable) accession number: P29019
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 16, 2013
This is version 67 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries