P40566 · EGH1_YEAST
- ProteinErgosteryl-beta-glucosidase
- GeneEGH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids764 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Ergosteryl beta-glucosidase involved in the ergosteryl beta-glucoside (EG) catabolic pathway and vacuole formation via hydrolysis of EG to generate glucose (PubMed:26116408).
Is also able to hydrolyze cholesteryl beta-glucoside and sitosteryl beta-glucoside to generate glucose; and C6-7-nitro-2,1,3-benzoxadiazole (NBD)-GlcCer to generate C6-NBD-ceramide (Cer) (PubMed:26116408).
Is also able to hydrolyze cholesteryl beta-glucoside and sitosteryl beta-glucoside to generate glucose; and C6-7-nitro-2,1,3-benzoxadiazole (NBD)-GlcCer to generate C6-NBD-ceramide (Cer) (PubMed:26116408).
Miscellaneous
Present with 1070 molecules/cell in log phase SD medium.
Catalytic activity
- ergosteryl 3-beta-D-glucoside + H2O = D-glucose + ergosterol
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 515 | Nucleophile | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | fungal-type vacuole membrane | |
Molecular Function | steryl-beta-glucosidase activity | |
Biological Process | ergosteryl 3-beta-D-glucoside catabolic process | |
Biological Process | polysaccharide catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameErgosteryl-beta-glucosidase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP40566
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Vacuole membrane ; Peripheral membrane protein
Note: Localizes in the cytosol until the initial logarithmic phase, then targets to a yet unidentified organelle with a granule structure in the middle logarithmic phase, and finally localizes at the vacuole membranes in the stationary phase.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Resulted in the accumulation of ergosteryl beta-glucoside (EG) and fragmentation of vacuoles.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 15 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000184056 | 1-764 | Ergosteryl-beta-glucosidase | |||
Sequence: MPAKIHISADGQFCDKDGNEIQLRGVNLDPSVKIPAKPFLSTHAPIENDTFFEDADKVSFINHPLVLDDIEQHIIRLKSLGYNTIRLPFTWESLEHAGPGQYDFDYMDYIVEVLTRINSVQQGMYIYLDPHQDVWSRFSGGSGAPLWTLYCAGFQPANFLATDAAILHNYYIDPKTGREVGKDEESYPKMVWPTNYFKLACQTMFTLFFGGKQYAPKCTINGENIQDYLQGRFNDAIMTLCARIKEKAPELFESNCIIGLESMNEPNCGYIGETNLDVIPKERNLKLGKTPTAFQSFMLGEGIECTIDQYKRTFFGFSKGKPCTINPKGKKAWLSAEERDAIDAKYNWERNPEWKPDTCIWKLHGVWEIQNGKRPVLLKPNYFSQPDATVFINNHFVDYYTGIYNKFREFDQELFIIIQPPVMKPPPNLQNSKILDNRTICACHFYDGMTLMYKTWNKRIGIDTYGLVNKKYSNPAFAVVLGENNIRKCIRKQLSEMQKDAKSMLGKKVPVFFTEIGIPFDMDDKKAYITNDYSSQTAALDALGFALEGSNLSYTLWCYCSINSHIWGDNWNNEDFSIWSPDDKPLYHDTRAKTPTPEPSPASTVASVSTSTSKSGSSQPPSFIKPDNHLDLDSPSCTLKSDLSGFRALDAIMRPFPIQIHGRFEFAEFNLCNKSYLLKLVGKTTPEQITVPTYIFIPRHHFTPSRLSIRSSSGHYTYNTDYQVLEWFHEPGHQFIEICAKSKSRPNTPGSDTSNDLPAECVIS | ||||||
Modified residue | 594 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 588-629 | Disordered | ||||
Sequence: HDTRAKTPTPEPSPASTVASVSTSTSKSGSSQPPSFIKPDNH | ||||||
Compositional bias | 596-624 | Polar residues | ||||
Sequence: TPEPSPASTVASVSTSTSKSGSSQPPSFI |
Sequence similarities
Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length764
- Mass (Da)86,979
- Last updated1995-02-01 v1
- Checksum7D22AFE3E8E9FF02
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 596-624 | Polar residues | ||||
Sequence: TPEPSPASTVASVSTSTSKSGSSQPPSFI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X79743 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
Z37996 EMBL· GenBank· DDBJ | CAA86077.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z38062 EMBL· GenBank· DDBJ | CAA86209.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006942 EMBL· GenBank· DDBJ | DAA08553.1 EMBL· GenBank· DDBJ | Genomic DNA |