Q74K42 · INUS_LACJO
- ProteinInulosucrase
- GeneinuJ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids797 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- [(2->1)-beta-D-fructosyl](n) + sucrose = [(2->1)-beta-D-fructosyl](n+1) + D-glucose
[(2→1)-β-D-fructosyl](n) RHEA-COMP:10036 + CHEBI:17992 = [(2→1)-β-D-fructosyl](n+1) RHEA-COMP:14296 + CHEBI:4167
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 271 | substrate | ||||
Sequence: W | ||||||
Active site | 272 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 317 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 340 | substrate | ||||
Sequence: S | ||||||
Binding site | 419 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 424-425 | substrate | ||||
Sequence: RD | ||||||
Site | 425 | Transition state stabilizer | ||||
Sequence: D | ||||||
Binding site | 450 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 487 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 489 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 521 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 522-524 | substrate | ||||
Sequence: EIE | ||||||
Active site | 524 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 542 | substrate | ||||
Sequence: R | ||||||
Binding site | 660 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 662 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 667 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | inulosucrase activity | |
Molecular Function | levansucrase activity | |
Molecular Function | metal ion binding | |
Biological Process | carbohydrate utilization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameInulosucrase
- EC number
- Short namesIS
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactobacillus
Accessions
- Primary accessionQ74K42
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Secreted, cell wall ; Peptidoglycan-anchor
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 272 | Loss of catalytic activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 301 | 25% of wild-type activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 301 | 40% of wild-type activity. | ||||
Sequence: N → S | ||||||
Mutagenesis | 301-303 | 1.5% of wild-type activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 305 | 29% of wild-type activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 305 | 50% of wild-type activity. | ||||
Sequence: N → S |
PTM/Processing
Features
Showing features for signal, chain, modified residue, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-36 | |||||
Sequence: MLENKNHKKISLSGKSLLMGTLSTAAIVLSASTANA | ||||||
Chain | PRO_0000431248 | 37-764 | Inulosucrase | |||
Sequence: ATINADNVNENQTVEVTASSVNNENNKQVTEKDSADKSTSDVAEDANTKKSNENTETTEKNTQTVVTNAPVSDVKNTNTVTAETPVDKVVNNSDQKTTNAATTDTKKDDVKQVEKKDSVDKTNAEENKDSSVKPAENATKAELKGQVKDIVEESGVDTSKLTNDQINELNKINFSKEAKSGTQLTYNDFKKIAKTLIEQDARYAIPFFNASKIKNMPAAKTLDAQSGKVEDLEIWDSWPVQDAKTGYVSNWNGYQLVIGMMGVPNVNDNHIYLLYNKYGDNDFNHWKNAGPIFGLGTPVIQQWSGSATLNKDGSIQLYYTKVDTSDNNTNHQKLASATVYLNLEKDQDKISIAHVDNDHIVFEGDGYHYQTYDQWKETNKGADNIAMRDAHVIDDDNGNRYLVFEASTGTENYQGDDQIYQWLNYGGTNKDNLGDFFQILSNSDIKDRAKWSNAAIGIIKLNDDVKNPSVAKVYSPLISAPMVSDEIERPDVVKLGNKYYLFAATRLNRGSNDDAWMATNKAVGDNVAMIGYVSDNLTHGYVPLNESGVVLTASVPANWRTATYSYYAVPVEGRDDQLLITSYITNRGEVAGKGMHATWAPSFLLQINPDNTTTVLAKMTNQGDWIWDDSSENPDMMGVLEKDAPNSAALPGEWGKPVDWDLIGGYNLKPHQPVTPIPNVPTTPETPTTPDKPEVPTTPEVPTTPETPTPEAPKNPVKKTSQSKLPKA | ||||||
Modified residue | 764 | Pentaglycyl murein peptidoglycan amidated alanine | ||||
Sequence: A | ||||||
Propeptide | PRO_0000431249 | 765-797 | Removed by sortase | |||
Sequence: GDKNSFAAVVLGAVSSILGAVGLTGVSKRKRNN |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 54-176 | Disordered | ||||
Sequence: ASSVNNENNKQVTEKDSADKSTSDVAEDANTKKSNENTETTEKNTQTVVTNAPVSDVKNTNTVTAETPVDKVVNNSDQKTTNAATTDTKKDDVKQVEKKDSVDKTNAEENKDSSVKPAENATK | ||||||
Compositional bias | 65-92 | Basic and acidic residues | ||||
Sequence: VTEKDSADKSTSDVAEDANTKKSNENTE | ||||||
Compositional bias | 93-136 | Polar residues | ||||
Sequence: TTEKNTQTVVTNAPVSDVKNTNTVTAETPVDKVVNNSDQKTTNA | ||||||
Compositional bias | 137-171 | Basic and acidic residues | ||||
Sequence: ATTDTKKDDVKQVEKKDSVDKTNAEENKDSSVKPA | ||||||
Region | 708-766 | Disordered | ||||
Sequence: QPVTPIPNVPTTPETPTTPDKPEVPTTPEVPTTPETPTPEAPKNPVKKTSQSKLPKAGD | ||||||
Compositional bias | 710-748 | Pro residues | ||||
Sequence: VTPIPNVPTTPETPTTPDKPEVPTTPEVPTTPETPTPEA | ||||||
Compositional bias | 750-764 | Polar residues | ||||
Sequence: KNPVKKTSQSKLPKA | ||||||
Motif | 761-765 | LPXTG sorting signal | ||||
Sequence: LPKAG |
Sequence similarities
Belongs to the glycosyl hydrolase 68 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length797
- Mass (Da)87,186
- Last updated2004-07-05 v1
- Checksum3E1F6460C93342C8
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 65-92 | Basic and acidic residues | ||||
Sequence: VTEKDSADKSTSDVAEDANTKKSNENTE | ||||||
Compositional bias | 93-136 | Polar residues | ||||
Sequence: TTEKNTQTVVTNAPVSDVKNTNTVTAETPVDKVVNNSDQKTTNA | ||||||
Compositional bias | 137-171 | Basic and acidic residues | ||||
Sequence: ATTDTKKDDVKQVEKKDSVDKTNAEENKDSSVKPA | ||||||
Compositional bias | 710-748 | Pro residues | ||||
Sequence: VTPIPNVPTTPETPTTPDKPEVPTTPEVPTTPETPTPEA | ||||||
Compositional bias | 750-764 | Polar residues | ||||
Sequence: KNPVKKTSQSKLPKA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE017198 EMBL· GenBank· DDBJ | AAS08734.1 EMBL· GenBank· DDBJ | Genomic DNA |