P95867 · TREZ_SACS2
- ProteinMalto-oligosyltrehalose trehalohydrolase
- GenetreZ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids561 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Catalytic activity
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
7.22 mM | maltotriosyltrehalose | |||||
5.66 mM | maltotetraosyltrehalose | |||||
5.89 mM | maltopentaosyltrehalose | |||||
5.86 mM | maltopentaose | |||||
5.63 mM | maltohexaose | |||||
2.63 mM | maltoheptaose |
pH Dependence
Optimum pH is 5.0.
Temperature Dependence
Optimum temperature is 85 degrees Celsius.
Pathway
Glycan biosynthesis; trehalose biosynthesis.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 253-258 | substrate | ||||
Sequence: RLDAVH | ||||||
Active site | 255 | Nucleophile | ||||
Sequence: D | ||||||
Active site | 286 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 311-315 | substrate | ||||
Sequence: DDFHH | ||||||
Binding site | 379-384 | substrate | ||||
Sequence: HDQVGN | ||||||
Site | 380 | Transition state stabilizer | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity | |
Biological Process | trehalose biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMalto-oligosyltrehalose trehalohydrolase
- EC number
- Short namesMTHase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Saccharolobus
Accessions
- Primary accessionP95867
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 218 | 15-fold and 150-fold reduction in specific activity, respectively. | ||||
Sequence: W → F or A | ||||||
Mutagenesis | 255 | 660-fold reduction in specific activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 259 | Insignificant change in specific activity. | ||||
Sequence: A → S | ||||||
Mutagenesis | 286 | 1100-fold reduction in specific activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 328 | 2-fold reduction in specific activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 355 | Very small decrease in specific activity. | ||||
Sequence: F → Y | ||||||
Mutagenesis | 356 | 2-fold reduction in specific activity. | ||||
Sequence: R → K | ||||||
Mutagenesis | 380 | 8140-fold reduction in specific activity. | ||||
Sequence: D → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000393752 | 1-561 | Malto-oligosyltrehalose trehalohydrolase | |||
Sequence: MTFGYKLDEDGVTFNLWAPYQRKVKLKILNRGIYEMERDDKGYFTITLDNVRVGDRYKYILDDNSEVPDPASRYQPEGVHGYSEIISPDFEWDDENSVKVKREDLVIYELHIGTFTSEGTFEGVIKKLNYLKELGVTAIEIMPIAQFPGKKDWGYDGVYLYAVQNSYGGPSGFRKLVNEAHKLGLAVILDVVYNHVGPEGNYMVKLGPYFSEKYKTPWGLTFNFDDAGSDEVRKFILENVEYWINEFHVDGFRLDAVHAIIDNSPKHILEDIADVVHKYDKIVIAESDLNDPRVVNPKEKCGYNIDAQWVDDFHHAIHAFLTGERQGYYSDFGSIGDIVKSYKDVFIYDGKYSNFRRKTHGKSVGDLDGCKFVVYIQNHDQVGNRGGGERLIKLVDKESYKIAAALYILSPYIPMIFMGEEYGEENPFYYFSDFSDPKLIQGVREGRRRENGQETDPQSDCTFNDSKLSWKINDDILSFYKSLIKIRKEYGLACNRKLSVENGNYWLTVKGNGCLAVYVFSKSVIEMKYSGTLVLSSNSSFPSQITESKYELDKGFALYKL |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length561
- Mass (Da)64,371
- Last updated1997-05-01 v1
- ChecksumB00E403020F6B242
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y08256 EMBL· GenBank· DDBJ | CAA69503.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE006641 EMBL· GenBank· DDBJ | AAK42272.1 EMBL· GenBank· DDBJ | Genomic DNA |