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Q43998 (SACB_GLUDI) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Levansucrase

EC=2.4.1.10
Alternative name(s):
Beta-D-fructofuranosyl transferase
Sucrose 6-fructosyl transferase
Gene names
Name:lsdA
OrganismGluconacetobacter diazotrophicus (Acetobacter diazotrophicus)
Taxonomic identifier33996 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter

Protein attributes

Sequence length584 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Releases fructooligosaccharides and levan, a high-molecular-mass fructosyl polymer, from sucrose. It acts more as a sucrose hydrolase than as a fructan polymerase.

Catalytic activity

Sucrose + (6)-beta-D-fructofuranosyl-(2->)(n) alpha-D-glucopyranoside = glucose + (6)-beta-D-fructofuranosyl-(2->)(n+1) alpha-D-glucopyranoside.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 68 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate utilization

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionlevansucrase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Propeptide31 – 5121
PRO_0000012245
Chain52 – 584533Levansucrase
PRO_0000012246

Amino acid modifications

Modified residue311Pyrrolidone carboxylic acid
Disulfide bond339 ↔ 395 Ref.2

Secondary structure

....................................................................................... 584
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q43998 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CBFBF4139AD0B8CE

FASTA58463,526
        10         20         30         40         50         60 
MAHVRRKVAT LNMALAGSLL MVLGAQSALA QGNFSRQEAA RMAHRPGVMP RGGPLFPGRS 

        70         80         90        100        110        120 
LAGVPGFPLP SIHTQQAYDP QSDFTARWTR ADALQIKAHS DATVAAGQNS LPAQLTMPNI 

       130        140        150        160        170        180 
PADFPVINPD VWVWDTWTLI DKHADQFSYN GWEVIFCLTA DPNAGYGFDD RHVHARIGFF 

       190        200        210        220        230        240 
YRRAGIPASR RPVNGGWTYG GHLFPDGASA QVYAGQTYTN QAEWSGSSRL MQIHGNTVSV 

       250        260        270        280        290        300 
FYTDVAFNRD ANANNITPPQ AIITQTLGRI HADFNHVWFT GFTAHTPLLQ PDGVLYQNGA 

       310        320        330        340        350        360 
QNEFFNFRDP FTFEDPKHPG VNYMVFEGNT AGQRGVANCT EADLGFRPND PNAETLQEVL 

       370        380        390        400        410        420 
DSGAYYQKAN IGLAIATDST LSKWKFLSPL ISANCVNDQT ERPQVYLHNG KYYIFTISHR 

       430        440        450        460        470        480 
TTFAAGVDGP DGVYGFVGDG IRSDFQPMNY GSGLTMGNPT DLNTAAGTDF DPSPDQNPRA 

       490        500        510        520        530        540 
FQSYSHYVMP GGLVESFIDT VENRRGGTLA PTVRVRIAQN ASAVDLRYGN GGLGGYGDIP 

       550        560        570        580 
ANRADVNIAG FIQDLFGQPT SGLAAQASTN NAQVLAQVRQ FLNQ 

« Hide

References

[1]"Molecular characterization of the levansucrase gene from the endophytic sugarcane bacterium Acetobacter diazotrophicus SRT4."
Arrieta J., Hernandez L., Coego A., Suarez V., Balmori E., Menendez C., Petit-Glatron M.-F., Chambert R., Selman-Housein G.
Microbiology 142:1077-1085(1996) [PubMed: 8704949] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 52-61.
Strain: SRT4 / CBS 550.94.
[2]"Structural characterization of Acetobacter diazotropicus levansucrase by matrix-assisted laser desorption/ionization mass spectrometry: identification of an N-terminal blocking group and a free-thiol cysteine residue."
Betancourt L., Takao T., Hernandez L., Padron G., Shimonishi Y.
J. Mass Spectrom. 34:169-174(1999) [PubMed: 10214721] [Abstract]
Cited for: DISULFIDE BOND, PYROGLUTAMATE FORMATION AT GLN-31.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L41732 Genomic DNA. Translation: AAB36606.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W18X-ray2.50A/B62-554[»]
ProteinModelPortalQ43998.
ModBaseSearch...

Protein family/group databases

CAZyGH68. Glycoside Hydrolase Family 68.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.65. 2464.

Family and domain databases

InterProIPR023296. Glyco_hydro_43_beta-prop.
IPR003469. Glyco_hydro_68.
[Graphical view]
Gene3DG3DSA:2.115.10.20. Glyco_hydro_43_beta-prop. 2 hits.
PfamPF02435. Glyco_hydro_68. 1 hit.
[Graphical view]
SUPFAMSSF75005. Glyco_hydro_43_beta-prop. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSACB_GLUDI
AccessionPrimary (citable) accession number: Q43998
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 64 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families