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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

    1. glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW
    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.

    C0HJE2-1 [UniParc]FASTAAdd to basket

    « Hide

            10
    SSNKLTTSWG
    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 (JUL-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.