Q74K42 · INUS_LACJO

Function

function

Fructosyltransferase that catalyzes the polymerization of the fructose moiety of sucrose to produce inulin polymer and inulin oligosaccharides such as 1-kestose and nystose.

Catalytic activity

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

pH Dependence

Optimum pH is 7. More than 85% of the activity is retained in the pH range 4.5-6.0. Activity decreases sharply at pH 7.5.

Temperature Dependence

Optimum temperature is 55 degrees Celsius. Activity drastically decreases at 60 degrees Celsius.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site271substrate
Active site272Nucleophile
Binding site317Ca2+ 1 (UniProtKB | ChEBI)
Binding site340substrate
Binding site419Ca2+ 2 (UniProtKB | ChEBI)
Binding site424-425substrate
Site425Transition state stabilizer
Binding site450Ca2+ 2 (UniProtKB | ChEBI)
Binding site487Ca2+ 2 (UniProtKB | ChEBI)
Binding site489Ca2+ 2 (UniProtKB | ChEBI)
Binding site521Ca2+ 2 (UniProtKB | ChEBI)
Binding site522-524substrate
Active site524Proton donor/acceptor
Binding site542substrate
Binding site660Ca2+ 1 (UniProtKB | ChEBI)
Binding site662Ca2+ 1 (UniProtKB | ChEBI)
Binding site667Ca2+ 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioninulosucrase activity
Molecular Functionlevansucrase activity
Molecular Functionmetal ion binding
Biological Processcarbohydrate utilization

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Inulosucrase
  • EC number
  • Short names
    IS

Gene names

    • Name
      inuJ
    • Synonyms
      ftf
    • Ordered locus names
      LJ_0913

Organism names

Accessions

  • Primary accession
    Q74K42

Proteomes

Subcellular Location

Secreted, cell wall
; Peptidoglycan-anchor

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis272Loss of catalytic activity.
Mutagenesis30125% of wild-type activity.
Mutagenesis30140% of wild-type activity.
Mutagenesis301-3031.5% of wild-type activity.
Mutagenesis30529% of wild-type activity.
Mutagenesis30550% of wild-type activity.

PTM/Processing

Features

Showing features for signal, chain, modified residue, propeptide.

TypeIDPosition(s)Description
Signal1-36
ChainPRO_000043124837-764Inulosucrase
Modified residue764Pentaglycyl murein peptidoglycan amidated alanine
PropeptidePRO_0000431249765-797Removed by sortase

Keywords

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region54-176Disordered
Compositional bias65-92Basic and acidic residues
Compositional bias93-136Polar residues
Compositional bias137-171Basic and acidic residues
Region708-766Disordered
Compositional bias710-748Pro residues
Compositional bias750-764Polar residues
Motif761-765LPXTG sorting signal

Sequence similarities

Belongs to the glycosyl hydrolase 68 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    797
  • Mass (Da)
    87,186
  • Last updated
    2004-07-05 v1
  • Checksum
    3E1F6460C93342C8
MLENKNHKKISLSGKSLLMGTLSTAAIVLSASTANAATINADNVNENQTVEVTASSVNNENNKQVTEKDSADKSTSDVAEDANTKKSNENTETTEKNTQTVVTNAPVSDVKNTNTVTAETPVDKVVNNSDQKTTNAATTDTKKDDVKQVEKKDSVDKTNAEENKDSSVKPAENATKAELKGQVKDIVEESGVDTSKLTNDQINELNKINFSKEAKSGTQLTYNDFKKIAKTLIEQDARYAIPFFNASKIKNMPAAKTLDAQSGKVEDLEIWDSWPVQDAKTGYVSNWNGYQLVIGMMGVPNVNDNHIYLLYNKYGDNDFNHWKNAGPIFGLGTPVIQQWSGSATLNKDGSIQLYYTKVDTSDNNTNHQKLASATVYLNLEKDQDKISIAHVDNDHIVFEGDGYHYQTYDQWKETNKGADNIAMRDAHVIDDDNGNRYLVFEASTGTENYQGDDQIYQWLNYGGTNKDNLGDFFQILSNSDIKDRAKWSNAAIGIIKLNDDVKNPSVAKVYSPLISAPMVSDEIERPDVVKLGNKYYLFAATRLNRGSNDDAWMATNKAVGDNVAMIGYVSDNLTHGYVPLNESGVVLTASVPANWRTATYSYYAVPVEGRDDQLLITSYITNRGEVAGKGMHATWAPSFLLQINPDNTTTVLAKMTNQGDWIWDDSSENPDMMGVLEKDAPNSAALPGEWGKPVDWDLIGGYNLKPHQPVTPIPNVPTTPETPTTPDKPEVPTTPEVPTTPETPTPEAPKNPVKKTSQSKLPKAGDKNSFAAVVLGAVSSILGAVGLTGVSKRKRNN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias65-92Basic and acidic residues
Compositional bias93-136Polar residues
Compositional bias137-171Basic and acidic residues
Compositional bias710-748Pro residues
Compositional bias750-764Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE017198
EMBL· GenBank· DDBJ
AAS08734.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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