A0R0W9 · TREH_MYCS2
- ProteinTrehalase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids668 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the hydrolysis of alpha,alpha-trehalose into two molecules of D-glucose. Does not hydrolyze maltose, isomaltose, sucrose, cellobiose, p-nitrophenyl-alpha-D-glucopyranoside, and methyl-alpha-D-glucopyranoside. Is also inactive on alpha,beta-trehalose, beta,beta-trehalose, alpha,alpha-trehalose-6,6'-dibehenate, trehalulose, nigerose, and trehalose dimycolate.
Catalytic activity
- alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Cofactor
Protein has several cofactor binding sites:
Note: Shows an absolute requirement for Mg2+ for activity. Mg2+ cannot be replaced by Ca2+, Mn2+ or Zn2+.
Note: Shows an absolute requirement for inorganic phosphate for activity. The function of the phosphate may involve stabilizing the protein conformation and/or initiating protein aggregation.
Activity regulation
Inhibited by pyrophosphate and polyphosphates. Also competitively inhibited by validoxylamine and castanospermine, but not by trehazolin.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
20 mM | alpha,alpha-trehalose |
pH Dependence
Optimum pH is 7.1. The trehalase activity drops sharply at pH values of 6.5 and below, as well as at pH values of 8.0 and above.
Pathway
Glycan degradation; trehalose degradation; D-glucose from alpha,alpha-trehalose: step 1/1.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | alpha,alpha-trehalase activity | |
Molecular Function | phosphate ion binding | |
Biological Process | trehalose catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTrehalase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionA0R0W9
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000413979 | 1-668 | Trehalase | |||
Sequence: MVLQQTEPTDGADRKASDGPLTVTAPVPYAAGPTLRNPFPPIADYGFLSDCETTCLISSAGSVEWLCVPRPDSPSVFGAILDRGAGHFRLGPYGVSVPAARRYLPGSLILETTWQTHTGWLIVRDALVMGPWHDIDTRSRTHRRTPMDWDAEHILLRTVRCVSGTVELVMSCEPAFDYHRVSATWEYSGPAYGEAIARASRNPDSHPTLRLTTNLRIGIEGREARARTRLTEGDNVFVALSWSKHPAPQTYEEAADKMWKTSEAWRQWINVGDFPDHPWRAYLQRSALTLKGLTYSPTGALLAAPTTSLPETPQGERNWDYRYSWIRDSTFALWGLYTLGLDREADDFFSFIADVSGANNGERHPLQVMYGVGGERSLVEEELHHLSGYDNSRPVRIGNGAYNQRQHDIWGTMLDSVYLHAKSREQIPDALWPVLKNQVEEAIKHWKEPDRGIWEVRGEPQHFTSSKIMCWVALDRGSKLAELQGEKSYAQQWRAIAEEIKADVLARGVDKRGVLTQRYGDDALDASLLLAVLTRFLPADDPRIRATVLAIADELTEDGLVLRYRVEETDDGLAGEEGTFTICSFWLVSALVEIGEISRAKHLCERLLSFASPLHLYAEEIEPRTGRHLGNFPQAFTHLALINAVVHVIRAEEEADSSGVFVPANAPM |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length668
- Mass (Da)74,690
- Last updated2007-01-09 v1
- Checksum22AE1581E85F503A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000480 EMBL· GenBank· DDBJ | ABK72415.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP001663 EMBL· GenBank· DDBJ | AFP40876.1 EMBL· GenBank· DDBJ | Genomic DNA |