A0A0N9MVA4 · A0A0N9MVA4_TALEM
- Proteinalpha-amylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids495 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
Function
Catalytic activity
Cofactor
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 101 | substrate | ||||
Sequence: W | ||||||
Binding site | 140 | substrate | ||||
Sequence: H | ||||||
Binding site | 222 | substrate | ||||
Sequence: R | ||||||
Active site | 224 | Nucleophile | ||||
Sequence: D | ||||||
Active site | 248 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 315 | substrate | ||||
Sequence: D | ||||||
Site | 315 | Transition state stabilizer | ||||
Sequence: D | ||||||
Binding site | 362 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | alpha-amylase activity | |
Molecular Function | calcium ion binding | |
Biological Process | carbohydrate catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namealpha-amylase
- EC number
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Trichocomaceae > Rasamsonia
Accessions
- Primary accessionA0A0N9MVA4
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MKLPLFIASTALTSAVLA | ||||||
Chain | PRO_5007420846 | 19-495 | alpha-amylase | |||
Sequence: ADAADWRSRSIYQLLTDRFSRPDGSTTAPCVTEDRRYCGGTFQGIIKQLDYIQRMGFTAIWISPVTHQLEGRTPYGEAYHGYWQQDLYKLNSHFGSPDDLRELAEELHRRDMYLMLDVVVNHNGWNGSASTVDYSVFHPFNKKEYYHDYCPILDWSNQTQVEDCWIGDNLVSCPDLYTQHPHVRREYQSWISDLVRDYSVDGLRIDTAREVEKDFFLGFVSASGVFATGEVMVNDANEACPYQPYLGSFLNYPAYYSLIDAFKSPSGNISSLVNQINLVKSTCLDTTVLGSFSENHDNPRFANYTADLSLAKNVIAFTMLADGIPIIYAGQEQHYSGGNDPNNREALWLSGYDTSAPLYQHVAQLNRLRSHAARQSPTYLTYKNQPIYSDSTTLAMRKGFDGQQVITVLSNLGTSGPKYVLSLGNTGYQRGQELVEVLTCTHVTVDDNGNVPVQMEQGLPRVFYPEHQLRGSGLCDL | ||||||
Disulfide bond | 48↔56 | |||||
Sequence: CVTEDRRYC | ||||||
Disulfide bond | 168↔182 | |||||
Sequence: CPILDWSNQTQVEDC | ||||||
Disulfide bond | 258↔301 | |||||
Sequence: CPYQPYLGSFLNYPAYYSLIDAFKSPSGNISSLVNQINLVKSTC | ||||||
Disulfide bond | 458↔493 | |||||
Sequence: CTHVTVDDNGNVPVQMEQGLPRVFYPEHQLRGSGLC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-387 | Glycosyl hydrolase family 13 catalytic | ||||
Sequence: QLLTDRFSRPDGSTTAPCVTEDRRYCGGTFQGIIKQLDYIQRMGFTAIWISPVTHQLEGRTPYGEAYHGYWQQDLYKLNSHFGSPDDLRELAEELHRRDMYLMLDVVVNHNGWNGSASTVDYSVFHPFNKKEYYHDYCPILDWSNQTQVEDCWIGDNLVSCPDLYTQHPHVRREYQSWISDLVRDYSVDGLRIDTAREVEKDFFLGFVSASGVFATGEVMVNDANEACPYQPYLGSFLNYPAYYSLIDAFKSPSGNISSLVNQINLVKSTCLDTTVLGSFSENHDNPRFANYTADLSLAKNVIAFTMLADGIPIIYAGQEQHYSGGNDPNNREALWLSGYDTSAPLYQHVAQLNRLR |
Sequence similarities
Belongs to the glycosyl hydrolase 13 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length495
- Mass (Da)55,716
- Last updated2016-01-20 v1
- ChecksumEDA3E69D6167E85B