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

C0HJE2 (AMYG_BACLI) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 2. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Glucoamylase

EC=3.2.1.3
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
OrganismBacillus licheniformis
Taxonomic identifier1402 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length10 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Ref.1

Miscellaneous

On the 2D-gel the determined pI of this protein is: 5.0, its MW is: 185 kDa. Ref.1

Biophysicochemical properties

Kinetic parameters:

Because of the indeterminate molecular weight of starch, an approximate KM value of 0.2178 mg/ml was determined. Ref.1

pH dependence:

Optimum pH is 5.0. Ref.1

Temperature dependence:

Optimum temperature is 50 degrees Celsius. Ref.1

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglucan 1,4-alpha-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›10›10Glucoamylase
PRO_0000424174

Experimental info

Non-terminal residue101

Sequences

Sequence LengthMass (Da)Tools
C0HJE2 [UniParc].

Last modified October 16, 2013. Version 1.
Checksum: 18FABAA1B1A72334

FASTA101,080
        10 
SSNKLTTSWG 

« Hide

References

[1]"Isolation, purification and characterization of glucoamylase from wild strain of Bacillus licheniformis KIBGE-IB3."
Ghani M., Rehman H.U., Siddiqui N.N., Aman A., Qader S.A.
Submitted (AUG-2013) to UniProtKB
Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: KIBGE-IB3.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameAMYG_BACLI
AccessionPrimary (citable) accession number: C0HJE2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: October 16, 2013
Last modified: December 11, 2013
This is version 2 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries