P0DJA3 · LSC_ZYMMO

Function

function

Catalyzes the synthesis of levan, a fructose polymer, by transferring the fructosyl moiety from sucrose to a growing acceptor molecule (PubMed:12359071).
Can also cleave raffinose and stachyose, but does not cleave 1-kestose, nystose, levan and inulin (PubMed:12359071).
Also displays sucrose hydrolase activity (PubMed:12359071).

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
125 mMsucrose
kcat is 1700 min-1 for sucrose hydrolase activity.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site47sucrose (UniProtKB | ChEBI)
Active site48Nucleophile
Binding site48sucrose (UniProtKB | ChEBI)
Binding site119sucrose (UniProtKB | ChEBI)
Binding site193sucrose (UniProtKB | ChEBI)
Binding site194sucrose (UniProtKB | ChEBI)
Site194Transition state stabilizer
Active site278Proton donor/acceptor

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionlevansucrase activity
Biological Processcarbohydrate utilization

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Levansucrase
  • EC number
  • Alternative names
    • Beta-D-fructofuranosyl transferase
    • Sucrose 6-fructosyl transferase

Gene names

    • Name
      sacB
    • Synonyms
      levU
      , sucZE2
    • Ordered locus names
      ZMO0374

Organism names

Accessions

  • Primary accession
    P0DJA3
  • Secondary accessions
    • Q06487
    • Q5NQK6
    • Q60114
    • Q60116

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis80Exhibits kinetic parameters and transfructosylation activity that are almost the same as those of the wild-type enzyme, but is unable to catalyze the synthesis of highly polymerized fructans.
Mutagenesis117Does not affect sucrose hydrolase activity. Exhibits greater transfructosylating activity.
Mutagenesis194Abolishes sucrose hydrolysis.
Mutagenesis194Abolishes sucrose hydrolysis. 3-fold increase in KM for sucrose. Transfructosylating activity is not affected.
Mutagenesis211Retains 28% of the sucrose hydrolase activity, but transfructosylating activity is greatly reduced.
Mutagenesis2238-fold increase in KM for sucrose. Shows higher activity toward stachyose.
Mutagenesis275No change in activity.
Mutagenesis27830-fold decrease in kcat for sucrose hydrolysis. KM for sucrose and transfructosylating activity are only slightly affected.
Mutagenesis278210-fold decrease in kcat for sucrose hydrolysis. 3-fold increase in KM for sucrose.
Mutagenesis296Decreases both transfructosylating and hydrolyzing activities.
Mutagenesis302No change in activity.
Mutagenesis308No change in activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000577211-423Levansucrase

Post-translational modification

Does not seem to be N-terminally processed.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyl hydrolase 68 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    423
  • Mass (Da)
    46,762
  • Last updated
    2011-12-14 v1
  • Checksum
    19A4691DA3EB9FE3
MLNKAGIAEPSLWTRADAMKVHTDDPTATMPTIDYDFPVMTDKYWVWDTWPLRDINGQVVSFQGWSVIFALVADRTKYGWHNRNDGARIGYFYSRGGSNWIFGGHLLKDGANPRSWEWSGCTIMAPGTANSVEVFFTSVNDTPSESVPAQCKGYIYADDKSVWFDGFDKVTDLFQADGLYYADYAENNFWDFRDPHVFINPEDGKTYALFEGNVAMERGTVAVGEEEIGPVPPKTETPDGARYCAAAIGIAQALNEARTEWKLLPPLVTAFGVNDQTERPHVVFQNGLTYLFTISHHSTYADGLSGPDGVYGFVSENGIFGPYEPLNGSGLVLGNPSSQPYQAYSHYVMTNGLVTSFIDTIPSSDPNVYRYGGTLAPTIKLELVGHRSFVTEVKGYGYIPPQIEWLAEDESSNSAAALSLLNK

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict39in Ref. 1; BAA04475
Sequence conflict200-203in Ref. 2; AAG29870
Sequence conflict217in Ref. 1; BAA04475
Sequence conflict220in Ref. 1; BAA04475
Sequence conflict244in Ref. 1; BAA04475
Sequence conflict379in Ref. 1; BAA04475

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D17524
EMBL· GenBank· DDBJ
BAA04475.1
EMBL· GenBank· DDBJ
Genomic DNA
AF313764
EMBL· GenBank· DDBJ
AAG29870.1
EMBL· GenBank· DDBJ
Genomic DNA
AE008692
EMBL· GenBank· DDBJ
AAV88998.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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