P0DJA3 · LSC_ZYMMO
- ProteinLevansucrase
- GenesacB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids423 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- [6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside + D-glucose
[6)-β-D-fructofuranosyl-(2→](n) α-D-glucopyranoside RHEA-COMP:13093 + CHEBI:17992 = [6)-β-D-fructofuranosyl-(2→](n+1) α-D-glucopyranoside RHEA-COMP:13094 + CHEBI:4167
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
125 mM | sucrose |
kcat is 1700 min-1 for sucrose hydrolase activity.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 47 | sucrose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Active site | 48 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 48 | sucrose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 119 | sucrose (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 193 | sucrose (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 194 | sucrose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 194 | Transition state stabilizer | ||||
Sequence: D | ||||||
Active site | 278 | Proton donor/acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | levansucrase activity | |
Biological Process | carbohydrate utilization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLevansucrase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Zymomonadaceae > Zymomonas
Accessions
- Primary accessionP0DJA3
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 80 | Exhibits 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. | ||||
Sequence: W → R | ||||||
Mutagenesis | 117 | Does not affect sucrose hydrolase activity. Exhibits greater transfructosylating activity. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 194 | Abolishes sucrose hydrolysis. | ||||
Sequence: D → A, E, H, Q, or S | ||||||
Mutagenesis | 194 | Abolishes sucrose hydrolysis. 3-fold increase in KM for sucrose. Transfructosylating activity is not affected. | ||||
Sequence: D → N | ||||||
Mutagenesis | 211 | Retains 28% of the sucrose hydrolase activity, but transfructosylating activity is greatly reduced. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 223 | 8-fold increase in KM for sucrose. Shows higher activity toward stachyose. | ||||
Sequence: V → A | ||||||
Mutagenesis | 275 | No change in activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 278 | 30-fold decrease in kcat for sucrose hydrolysis. KM for sucrose and transfructosylating activity are only slightly affected. | ||||
Sequence: E → D | ||||||
Mutagenesis | 278 | 210-fold decrease in kcat for sucrose hydrolysis. 3-fold increase in KM for sucrose. | ||||
Sequence: E → H | ||||||
Mutagenesis | 296 | Decreases both transfructosylating and hydrolyzing activities. | ||||
Sequence: H → K or R | ||||||
Mutagenesis | 302 | No change in activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 308 | No change in activity. | ||||
Sequence: D → N |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000057721 | 1-423 | Levansucrase | |||
Sequence: MLNKAGIAEPSLWTRADAMKVHTDDPTATMPTIDYDFPVMTDKYWVWDTWPLRDINGQVVSFQGWSVIFALVADRTKYGWHNRNDGARIGYFYSRGGSNWIFGGHLLKDGANPRSWEWSGCTIMAPGTANSVEVFFTSVNDTPSESVPAQCKGYIYADDKSVWFDGFDKVTDLFQADGLYYADYAENNFWDFRDPHVFINPEDGKTYALFEGNVAMERGTVAVGEEEIGPVPPKTETPDGARYCAAAIGIAQALNEARTEWKLLPPLVTAFGVNDQTERPHVVFQNGLTYLFTISHHSTYADGLSGPDGVYGFVSENGIFGPYEPLNGSGLVLGNPSSQPYQAYSHYVMTNGLVTSFIDTIPSSDPNVYRYGGTLAPTIKLELVGHRSFVTEVKGYGYIPPQIEWLAEDESSNSAAALSLLNK |
Post-translational modification
Does not seem to be N-terminally processed.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length423
- Mass (Da)46,762
- Last updated2011-12-14 v1
- Checksum19A4691DA3EB9FE3
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 39 | in Ref. 1; BAA04475 | ||||
Sequence: V → I | ||||||
Sequence conflict | 200-203 | in Ref. 2; AAG29870 | ||||
Sequence: NPED → TPKI | ||||||
Sequence conflict | 217 | in Ref. 1; BAA04475 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 220 | in Ref. 1; BAA04475 | ||||
Sequence: T → A | ||||||
Sequence conflict | 244 | in Ref. 1; BAA04475 | ||||
Sequence: C → Y | ||||||
Sequence conflict | 379 | in Ref. 1; BAA04475 | ||||
Sequence: I → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |