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Reviewed, UniProtKB/Swiss-Prot P29019 (GUN_BACSZ)

Last modified June 16, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

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: 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
P29019-1 [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: 1770347] [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: 2045781] [Abstract]
Cited for: PROTEIN SEQUENCE OF 56-75, CHARACTERIZATION.

Cross-references

Sequence databases

M68872 Genomic DNA. Translation: AAA22409.1.
PIRA44808.

3D structure databases

HSSPHSSP built from PDB template 1IS9 based on UniProtKB P04955.
SMRP29019. Positions 57-442.
ModBaseSearch...

Protein family/group databases

CAZyGH8. Glycoside Hydrolase Family 8.

Family and domain databases

InterProIPR012341. 6hp_glycosidase.
IPR002037. Glyco_hydro_8.
IPR019834. Glyco_hydro_8_CS.
[Graphical view]
Gene3DG3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
PfamPF01270. Glyco_hydro_8. 1 hit.
[Graphical view]
PRINTSPR00735. GLHYDRLASE8.
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: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents