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Protein

Glucoamylase

Gene
N/A
Organism
Bacillus licheniformis
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Kineticsi

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

      pH dependencei

      Optimum pH is 5.0.1 Publication

      Temperature dependencei

      Optimum temperature is 50 degrees Celsius.1 Publication

      GO - Molecular functioni

      GO - Biological processi

      Complete GO annotation...

      Keywords - Molecular functioni

      Glycosidase, Hydrolase

      Keywords - Biological processi

      Carbohydrate metabolism, Polysaccharide degradation

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Glucoamylase1 Publication (EC:3.2.1.31 Publication)
      Alternative name(s):
      1,4-alpha-D-glucan glucohydrolaseBy similarity
      Glucan 1,4-alpha-glucosidaseBy similarity
      OrganismiBacillus licheniformis
      Taxonomic identifieri1402 [NCBI]
      Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – ›10›10GlucoamylasePRO_0000424174

      Sequencei

      Sequence statusi: Fragment.

      Length:10
      Mass (Da):1,080
      Last modified:October 16, 2013 - v1
      Checksum:i18FABAA1B1A72334
      GO

      Experimental Info

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Non-terminal residuei10 – 1011 Publication

      Cross-referencesi

      3D structure databases

      ModBaseiSearch...
      MobiDBiSearch...

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Family and domain databases

      ProtoNetiSearch...

      Publicationsi

      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-IB31 Publication.

      Entry informationi

      Entry nameiAMYG_BACLI
      AccessioniPrimary (citable) accession number: C0HJE2
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: October 16, 2013
      Last sequence update: October 16, 2013
      Last modified: October 1, 2014
      This is version 3 of the entry and version 1 of the sequence. [Complete history]
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programProkaryotic Protein Annotation Program

      Miscellaneousi

      Miscellaneous

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

      Keywords - Technical termi

      Direct protein sequencing

      Documents

      1. Glycosyl hydrolases
        Classification of glycosyl hydrolase families and list of entries

      External Data

      Dasty 3

      Similar proteinsi

      Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
      100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
      90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
      50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.