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P85080 (GTF3_LEUME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Dextransucrase

EC=2.4.1.5
Alternative name(s):
Glucansucrase
Sucrose 6-glucosyltransferase
OrganismLeuconostoc mesenteroides
Taxonomic identifier1245 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLeuconostoc

Protein attributes

Sequence length6 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the production of dextran, an extracellular glucan polymer. Ref.1

Catalytic activity

Sucrose + ((1->6)-alpha-D-glucosyl)(n) = D-fructose + ((1->6)-alpha-D-glucosyl)(n+1). Ref.1

Miscellaneous

Synthesizes water-soluble glucans (alpha 1,6-glucose). Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 70 family.

Biophysicochemical properties

Kinetic parameters:

KM=69.88 mM for sucrose Ref.1

pH dependence:

Optimum pH is 5.0. Ref.1

Temperature dependence:

Optimum temperature is 35 degrees Celsius. Ref.1

Ontologies

Keywords
   Molecular functionGlycosyltransferase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functiondextransucrase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›6›6Dextransucrase
PRO_0000284553

Experimental info

Non-terminal residue61

Sequences

Sequence LengthMass (Da)Tools
P85080 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: 72D1A451B5BAC000

FASTA6636
DSTNTV 

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References

[1]"Purification and characterization of glucansucrase from Leuconostoc mesentriodes AA1."
Aman A., Ul Qader S.A., Azhar A., Syed M.N.
Submitted (JAN-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: AA1.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameGTF3_LEUME
AccessionPrimary (citable) accession number: P85080
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: April 16, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries