M1RNJ8 · ATH1_CANGB

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).

Catalytic activity

Features

Showing features for binding site, active site.

112121002003004005006007008009001,0001,1001,200
TypeIDPosition(s)Description
Binding site546-547substrate
Active site677Proton donor
Binding site744-745substrate

GO annotations

AspectTerm
Cellular Componentcell wall-bounded periplasmic space
Cellular Componentextracellular region
Cellular Componentfungal-type cell wall
Cellular Componentfungal-type vacuole lumen
Cellular Componentmembrane
Cellular Componentperiplasmic space
Molecular Functionalpha,alpha-trehalase activity
Molecular Functioncarbohydrate binding
Biological Processcarbon utilization
Biological Processtrehalose catabolic process
Biological Processtrehalose transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Periplasmic/secreted acid trehalase ATH1
  • EC number
  • Short names
    cgATH1

Gene names

    • Name
      ATH1

Organism names

Accessions

  • Primary accession
    M1RNJ8

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-82Cytoplasmic
Transmembrane83-103Helical
Topological domain104-1212Periplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

Abolishes growth in trehalose carbon source (PubMed:33146242).
Normal growth in glucose carbon source (PubMed:33146242).
Decreases virulence in a mouse infection model (PubMed:33146242).

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00004523291-1212Periplasmic/secreted acid trehalase ATH1
Glycosylation243N-linked (GlcNAc...) asparagine
Glycosylation275N-linked (GlcNAc...) asparagine
Glycosylation296N-linked (GlcNAc...) asparagine
Glycosylation362N-linked (GlcNAc...) asparagine
Glycosylation414N-linked (GlcNAc...) asparagine
Glycosylation428N-linked (GlcNAc...) asparagine
Glycosylation521N-linked (GlcNAc...) asparagine
Glycosylation572N-linked (GlcNAc...) asparagine
Glycosylation601N-linked (GlcNAc...) asparagine
Glycosylation661N-linked (GlcNAc...) asparagine
Glycosylation671N-linked (GlcNAc...) asparagine
Glycosylation729N-linked (GlcNAc...) asparagine
Glycosylation738N-linked (GlcNAc...) asparagine
Glycosylation912N-linked (GlcNAc...) asparagine
Glycosylation938N-linked (GlcNAc...) asparagine
Glycosylation993N-linked (GlcNAc...) asparagine
Glycosylation1011N-linked (GlcNAc...) asparagine
Glycosylation1033N-linked (GlcNAc...) asparagine
Glycosylation1052N-linked (GlcNAc...) asparagine
Glycosylation1070N-linked (GlcNAc...) asparagine
Glycosylation1097N-linked (GlcNAc...) asparagine
Glycosylation1165N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyl hydrolase 65 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,212
  • Mass (Da)
    136,519
  • Last updated
    2013-05-01 v1
  • Checksum
    2DB70E1AB18662C9
MGFKDKILFWKDEVQYRTLAVADQVANRFLHSFENVYQGDESVEDADSRPVGLTNETLSHSSDFFVLPEERISTRVKIRRQNILNTTLILGMLIALVIWTAILSTNSYFSSSLASASPLFNKEGRVVRPMRESNLGLHADPQTRKSSKTLYDLLSDFDNAFYDDENMILGSLAFGENTYSRQPYVANGYIGSRIPNIGFGYALDTLNLYADAPGALNNGWPLRNRRFAGSFVSDFYSLQAKLNSTNFPELDEKGYTTVISSIPEWTDLQFTVDLNGTKWFNPQSVLIDDVINYNQNLSMKDGIVSTNMDWLNGMINIKSEVWAHRKIHSLGITRLEISLNLDALPDEFTELPVTVYDIIDLNTSHRTTLYEKGQDEDNKAIYMIVNPDNVPYSNAVVYSTCTIKGTENNFSPYNFTSDDRIARNYMTNLTEENPKVVIYKYTSVVSSEYNNDEPNPNVNLKFASNIANTAKGNYKSLLSNHKRAWYDLYNDAFIEIPSDSLLEMTARSSLFHLLANTRQYNVSTTRGLPVGVGGLSSDSYGGMVFWDADVWMAPALLPFFPNIAMNMNNYRNATHQQAIENAKQYNYPGAVYPWTSGRYANCTSTGPCIDYEYHINVDIALASFSIYMNGAEGADEDYLRFTTWPMVKDAAVFFKAYVKYNETLGEYETYNLTDPDEFANHVNNGAFTNAGIKTLLKWATDIGTHLGEEVDPKWMEIADNIHIPRSDSNITLEYSGMNSSVEIKQADVTLMVYPLGYINDESILNNAIKDLYYYSERQSASGPAMTYPVFVAAAASLLNHGSSSQSYLYKSVLPYLRSPFAQFSEQSDDNFLTNGLTQPAFPFLTANGGFLQSILFGLTGLRYSYEVTPRTKKISRLLKFDPVKLPLLPGGIAIRNFKYMGQVLDIIIDDNNGTIAHKGGDKPIRIKVPNRDILHDRNITSALYSKRDDDLSATDDYYGTYFTLYPNEELVIPLYDTKLNIDGNIAESKQITNLTAGVPGDVGFSALDGNNYTHWQPFDKSDNAKLLIDLGFNSTHVIKKGIILWGQRPAKNISLSVLPHSERIEQLFANITDLLETSSITKGGLPLNQMLGQTQSNVTAEIDDDILALLNWKGDDLDQLIPYLPDMHLLQEKFIPILKDYPIKPNQRYYEEIIDDDIIKLLPSNTTEFTIDYNSIPGGEKRARYVVLTVHGTYDDDDDLKGATIREIVLQE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KC208027
EMBL· GenBank· DDBJ
AGG12634.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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