Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dextranase

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

Functioni

Catalytic activityi

Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in dextran.1 Publication

Kineticsi

Because of the indeterminate molecular weight of dextran, an approximate KM value of 0.3738 mg/ml was determined.1 Publication

      pH dependencei

      Optimum pH is 4.5.1 Publication

      Temperature dependencei

      Optimum temperature is 35 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:
      Dextranase1 Publication (EC:3.2.1.111 Publication)
      Alternative name(s):
      Alpha-1,6-glucan-6-glucanohydrolaseBy similarity
      OrganismiBacillus licheniformis
      Taxonomic identifieri1402 [NCBI]
      Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – ›10›10DextranasePRO_0000424175

      Sequencei

      Sequence statusi: Fragment.

      Length:10
      Mass (Da):1,128
      Last modified:October 16, 2013 - v1
      Checksum:i924BD23B5731B2D1
      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. "Dextranase: isolation, purification and characterization of dextran degrading enzyme from Bacillus licheniformis KIBGE-IB25."
        Zohra R.R., Sattar H., Karim A., Aman A., Qader S.A.
        Submitted (AUG-2013) to UniProtKB
        Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
        Strain: KIBGE-IB251 Publication.

      Entry informationi

      Entry nameiDEXT_BACLI
      AccessioniPrimary (citable) accession number: C0HJE3
      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: 4.5, its MW is: 158 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.