Q11129 · MEL_SACMI
- ProteinAlpha-galactosidase
- GeneMEL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids471 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 72 | substrate | ||||
Sequence: D | ||||||
Binding site | 73 | substrate | ||||
Sequence: D | ||||||
Binding site | 147 | substrate | ||||
Sequence: K | ||||||
Active site | 149 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 205 | substrate | ||||
Sequence: R | ||||||
Active site | 209 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 251 | substrate | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Molecular Function | alpha-galactosidase activity | |
Biological Process | glycoside catabolic process | |
Biological Process | melibiose catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-galactosidase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ11129
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MSYIYLFITAAAVTGALG | ||||||
Chain | PRO_0000001007 | 19-471 | Alpha-galactosidase | |||
Sequence: SSPSYNGLGLTPQMGWDNWNTFACDVSEQLLLNTADRISEIGLKDLGYKYVILDDCWSSGRNSNGTLVADKNKFPNGMDHVARHLHNNNFLFGMYSSAGEYTCAGYPGSLGHEQEDAEFFARNGVDYLKYDNCYNKGKFGTPETSYKRYKAMSDALNKTGRPIFYSLCNWGQDLTFYWGSDIANSWRMSGDIYPEFDRPDSRCPCDGDQYDCSYAGFHCSIMNILNKAAPMGQNAGIGGWNDLDNLEVGVGNLTDDEEKAHFSMWAMVKSPLIIGADVNHLKESSYSIYSQASVIAINQDPKGVPATRVWRHYVSQTDKYGKGEIQLWSCPLDNGDQVIALLNGSNKKRPMNASLEDIFFDSYLGSEELSSSWDIYDLWANRIDNTIASNILKNNKVTNSSLYNATELSYKEGLSKNDTRLFGVQIGTVSPGGLLNTTVPAHGVALYRLRRSR | ||||||
Disulfide bond | 42↔74 | |||||
Sequence: CDVSEQLLLNTADRISEIGLKDLGYKYVILDDC | ||||||
Glycosylation | 82 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 121↔151 | |||||
Sequence: CAGYPGSLGHEQEDAEFFARNGVDYLKYDNC | ||||||
Glycosylation | 175 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 221↔237 | |||||
Sequence: CPCDGDQYDCSYAGFHC | ||||||
Disulfide bond | 223↔230 | |||||
Sequence: CDGDQYDC | ||||||
Glycosylation | 270 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 361 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 370 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 417 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 422 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 435 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 454 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length471
- Mass (Da)52,378
- Last updated1996-11-01 v1
- Checksum9FFF2FA03C03872A