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B0XT09 · GEL3_ASPFC

Function

function

Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis (By similarity).

Features

Showing features for binding site, active site.

154750100150200250300350400450500
Type
IDPosition(s)Description
Binding site86(1,3-beta-D-glucosyl)n 1 (UniProtKB | ChEBI); donor substrate
Binding site154(1,3-beta-D-glucosyl)n 1 (UniProtKB | ChEBI); donor substrate
Active site155Proton donor
Binding site155(1,3-beta-D-glucosyl)n 2 (UniProtKB | ChEBI); acceptor substrate
Binding site197(1,3-beta-D-glucosyl)n 2 (UniProtKB | ChEBI); acceptor substrate
Binding site202(1,3-beta-D-glucosyl)n 2 (UniProtKB | ChEBI); acceptor substrate
Active site257Nucleophile
Binding site289(1,3-beta-D-glucosyl)n 1 (UniProtKB | ChEBI); donor substrate

GO annotations

AspectTerm
Cellular Componentplasma membrane
Cellular Componentside of membrane
Molecular Function1,3-beta-glucanosyltransferase activity
Biological Processfungal-type cell wall (1->3)-beta-D-glucan biosynthetic process
Biological Processfungal-type cell wall organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    1,3-beta-glucanosyltransferase gel3
  • EC number
  • Alternative names
    • Glucan elongating glucanosyltransferase 3

Gene names

    • Name
      gel3
    • ORF names
      AFUB_028470

Organism names

Accessions

  • Primary accession
    B0XT09
  • Secondary accessions
    • Q4X0N8
    • Q9P8U3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond, lipidation, propeptide.

Type
IDPosition(s)Description
Signal1-20
ChainPRO_000037260721-5151,3-beta-glucanosyltransferase gel3
Glycosylation28N-linked (GlcNAc...) asparagine
Disulfide bond68↔97
Glycosylation161N-linked (GlcNAc...) asparagine
Disulfide bond211↔343
Disulfide bond229↔260
Glycosylation241N-linked (GlcNAc...) asparagine
Disulfide bond366↔419
Disulfide bond375↔443
Disulfide bond394↔401
Glycosylation407N-linked (GlcNAc...) asparagine
Lipidation515GPI-like-anchor amidated alanine
PropeptidePRO_0000372608516-547Removed in mature form

Post-translational modification

The GPI-like anchor contains a phosphoceramide lipid group.

Keywords

PTM databases

Structure

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias471-486Polar residues
Region471-503Disordered

Sequence similarities

Belongs to the glycosyl hydrolase 72 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    547
  • Mass (Da)
    57,218
  • Last updated
    2008-04-08 v1
  • MD5 Checksum
    7258F6DAE06784CB32E314F83A192F86
MRYSLVVGVVLLSGCAIATGSKFFYANNGSEFYIRGVAYQEDYSGGGAGGTGQSEANYVDPLADGSKCERDIPYLLQLRTNVIRTYAVNPSLNHDACMQKLSDAGIYVITDLASPDESITSNSPVWTVDQYARYTSVIDAFQKYDNVIGFFAGNEVVNQANQSAGAAFVKAAARDMKAYIKTKGYRQSLAIGYATTDNPEIRLPLSDYLNCGDQADAVDFFGYNIYEWCGDKTFQTSGYQNRTEEYKDYSIPIFFSEYGCNTEKPRKFTDVPVLFGPQMDNVWSGGIVYMYFETTNDYGLVSVSGSAVTPEPDFTYLSSEIQSATPTGVNSASYSPTNSPRACPTVDDTWLAKSSPLPPIPNAELCSCMVSSLSCVVKDSVDAEKYGELFGQVCGYGGGICDGIARNATAGSYGAYSVCTSKDQLSYVFDRYYKSQKKAASACDFAGAASVQSPKGESADCKSLVSQAGSAGTGTVTSQPTGGSGSTGGGGGGGGGGGGGGGAAASTSTSKGAAAGAASPAAVRVGGWPLVTYGLVAAMAGILMISL

Sequence caution

The sequence AAF40140.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias, sequence conflict.

Type
IDPosition(s)Description
Compositional bias471-486Polar residues
Sequence conflict485in Ref. 1; AAF40140
Sequence conflict502in Ref. 1; AAF40140

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF208040
EMBL· GenBank· DDBJ
AAF40140.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
DS499595
EMBL· GenBank· DDBJ
EDP54787.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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