M1RNJ8 · ATH1_CANGB
- ProteinPeriplasmic/secreted acid trehalase ATH1
- GeneATH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1212 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Periplasmic/secreted acid trehalase that catalyzes hydrolysis of the disaccharide trehalose and required for growth on trehalose as carbon source (PubMed:26411890, PubMed:33146242).
Growth on trehalose is not restricted to respiration (PubMed:26411890).
Growth on trehalose is not restricted to respiration (PubMed:26411890).
Catalytic activity
- alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 546-547 | substrate | ||||
Sequence: WD | ||||||
Active site | 677 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 744-745 | substrate | ||||
Sequence: KQ |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell wall-bounded periplasmic space | |
Cellular Component | extracellular region | |
Cellular Component | fungal-type cell wall | |
Cellular Component | fungal-type vacuole lumen | |
Cellular Component | membrane | |
Cellular Component | periplasmic space | |
Molecular Function | alpha,alpha-trehalase activity | |
Molecular Function | carbohydrate binding | |
Biological Process | carbon utilization | |
Biological Process | trehalose catabolic process | |
Biological Process | trehalose transport |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeriplasmic/secreted acid trehalase ATH1
- EC number
- Short namescgATH1
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Nakaseomyces
Accessions
- Primary accessionM1RNJ8
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-82 | Cytoplasmic | ||||
Sequence: MGFKDKILFWKDEVQYRTLAVADQVANRFLHSFENVYQGDESVEDADSRPVGLTNETLSHSSDFFVLPEERISTRVKIRRQN | ||||||
Transmembrane | 83-103 | Helical | ||||
Sequence: ILNTTLILGMLIALVIWTAIL | ||||||
Topological domain | 104-1212 | Periplasmic | ||||
Sequence: STNSYFSSSLASASPLFNKEGRVVRPMRESNLGLHADPQTRKSSKTLYDLLSDFDNAFYDDENMILGSLAFGENTYSRQPYVANGYIGSRIPNIGFGYALDTLNLYADAPGALNNGWPLRNRRFAGSFVSDFYSLQAKLNSTNFPELDEKGYTTVISSIPEWTDLQFTVDLNGTKWFNPQSVLIDDVINYNQNLSMKDGIVSTNMDWLNGMINIKSEVWAHRKIHSLGITRLEISLNLDALPDEFTELPVTVYDIIDLNTSHRTTLYEKGQDEDNKAIYMIVNPDNVPYSNAVVYSTCTIKGTENNFSPYNFTSDDRIARNYMTNLTEENPKVVIYKYTSVVSSEYNNDEPNPNVNLKFASNIANTAKGNYKSLLSNHKRAWYDLYNDAFIEIPSDSLLEMTARSSLFHLLANTRQYNVSTTRGLPVGVGGLSSDSYGGMVFWDADVWMAPALLPFFPNIAMNMNNYRNATHQQAIENAKQYNYPGAVYPWTSGRYANCTSTGPCIDYEYHINVDIALASFSIYMNGAEGADEDYLRFTTWPMVKDAAVFFKAYVKYNETLGEYETYNLTDPDEFANHVNNGAFTNAGIKTLLKWATDIGTHLGEEVDPKWMEIADNIHIPRSDSNITLEYSGMNSSVEIKQADVTLMVYPLGYINDESILNNAIKDLYYYSERQSASGPAMTYPVFVAAAASLLNHGSSSQSYLYKSVLPYLRSPFAQFSEQSDDNFLTNGLTQPAFPFLTANGGFLQSILFGLTGLRYSYEVTPRTKKISRLLKFDPVKLPLLPGGIAIRNFKYMGQVLDIIIDDNNGTIAHKGGDKPIRIKVPNRDILHDRNITSALYSKRDDDLSATDDYYGTYFTLYPNEELVIPLYDTKLNIDGNIAESKQITNLTAGVPGDVGFSALDGNNYTHWQPFDKSDNAKLLIDLGFNSTHVIKKGIILWGQRPAKNISLSVLPHSERIEQLFANITDLLETSSITKGGLPLNQMLGQTQSNVTAEIDDDILALLNWKGDDLDQLIPYLPDMHLLQEKFIPILKDYPIKPNQRYYEEIIDDDIIKLLPSNTTEFTIDYNSIPGGEKRARYVVLTVHGTYDDDDDLKGATIREIVLQE |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452329 | 1-1212 | Periplasmic/secreted acid trehalase ATH1 | |||
Sequence: MGFKDKILFWKDEVQYRTLAVADQVANRFLHSFENVYQGDESVEDADSRPVGLTNETLSHSSDFFVLPEERISTRVKIRRQNILNTTLILGMLIALVIWTAILSTNSYFSSSLASASPLFNKEGRVVRPMRESNLGLHADPQTRKSSKTLYDLLSDFDNAFYDDENMILGSLAFGENTYSRQPYVANGYIGSRIPNIGFGYALDTLNLYADAPGALNNGWPLRNRRFAGSFVSDFYSLQAKLNSTNFPELDEKGYTTVISSIPEWTDLQFTVDLNGTKWFNPQSVLIDDVINYNQNLSMKDGIVSTNMDWLNGMINIKSEVWAHRKIHSLGITRLEISLNLDALPDEFTELPVTVYDIIDLNTSHRTTLYEKGQDEDNKAIYMIVNPDNVPYSNAVVYSTCTIKGTENNFSPYNFTSDDRIARNYMTNLTEENPKVVIYKYTSVVSSEYNNDEPNPNVNLKFASNIANTAKGNYKSLLSNHKRAWYDLYNDAFIEIPSDSLLEMTARSSLFHLLANTRQYNVSTTRGLPVGVGGLSSDSYGGMVFWDADVWMAPALLPFFPNIAMNMNNYRNATHQQAIENAKQYNYPGAVYPWTSGRYANCTSTGPCIDYEYHINVDIALASFSIYMNGAEGADEDYLRFTTWPMVKDAAVFFKAYVKYNETLGEYETYNLTDPDEFANHVNNGAFTNAGIKTLLKWATDIGTHLGEEVDPKWMEIADNIHIPRSDSNITLEYSGMNSSVEIKQADVTLMVYPLGYINDESILNNAIKDLYYYSERQSASGPAMTYPVFVAAAASLLNHGSSSQSYLYKSVLPYLRSPFAQFSEQSDDNFLTNGLTQPAFPFLTANGGFLQSILFGLTGLRYSYEVTPRTKKISRLLKFDPVKLPLLPGGIAIRNFKYMGQVLDIIIDDNNGTIAHKGGDKPIRIKVPNRDILHDRNITSALYSKRDDDLSATDDYYGTYFTLYPNEELVIPLYDTKLNIDGNIAESKQITNLTAGVPGDVGFSALDGNNYTHWQPFDKSDNAKLLIDLGFNSTHVIKKGIILWGQRPAKNISLSVLPHSERIEQLFANITDLLETSSITKGGLPLNQMLGQTQSNVTAEIDDDILALLNWKGDDLDQLIPYLPDMHLLQEKFIPILKDYPIKPNQRYYEEIIDDDIIKLLPSNTTEFTIDYNSIPGGEKRARYVVLTVHGTYDDDDDLKGATIREIVLQE | ||||||
Glycosylation | 243 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 275 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 296 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 362 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 414 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 428 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 521 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 572 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 601 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 661 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 671 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 729 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 738 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 912 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 938 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 993 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1011 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1033 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1052 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1070 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1097 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1165 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length1,212
- Mass (Da)136,519
- Last updated2013-05-01 v1
- Checksum2DB70E1AB18662C9