Q1R5J5 · GLGX_ECOUT

Function

function

Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin.

Catalytic activity

  • Hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit dextrin.
    EC:3.2.1.196 (UniProtKB | ENZYME | Rhea)

Pathway

Glycan degradation; glycogen degradation.

Features

Showing features for active site, site.

165750100150200250300350400450500550600650
TypeIDPosition(s)Description
Active site336Nucleophile
Active site371Proton donor
Site443Transition state stabilizer

GO annotations

AspectTerm
Molecular Functionglycogen debranching enzyme activity
Molecular Functionhydrolase activity, hydrolyzing O-glycosyl compounds
Biological Processglycogen catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • CBM48Carbohydrate-Binding Module Family 48
    • GH13Glycoside Hydrolase Family 13

Names & Taxonomy

Protein names

  • Recommended name
    Glycogen debranching enzyme
  • EC number
  • Alternative names
    • Limit dextrin alpha-1,6-maltotetraose-hydrolase

Gene names

    • Name
      glgX
    • Ordered locus names
      UTI89_C3940

Organism names

Accessions

  • Primary accession
    Q1R5J5

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000671021-657Glycogen debranching enzyme

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region460-479Disordered
Compositional bias465-479Polar residues

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    657
  • Mass (Da)
    73,750
  • Last updated
    2006-05-16 v1
  • Checksum
    A2531483B04C463F
MTQLAIGKPTPLGAHYDGQGVNFTLFSAHAERVELCVFDANGQEHRYDLPGHSGDIWHGYLPDARPGLRYGYRVHGPWQPAEGHRFNPAKLLIDPCARQIDGEFKDNPLLHAGHNEPDYRDNASIAPKCVVVVDHYDWEDDAPPRMPWGCTIIYEAHVKGLTYLHPEIPVEIRGTYKALGHPVMINYLKQLGITALELLPVAQFASEPRLQRMGLSNYWGYNPVAMFALHPAYACSPETALDEFRDAIKALHKAGIEVILDIVLNHSAELDLDGPLFSLRGIDNRSYYWIREDGDYHNWTGCGNTLNLSHPAVVDYASACLRYWVETCHVDGFRFDLAAVMGRTPEFRQDALLFTAIQNCPVLSQVKLIAEPWDIAPGGYQVGNFPPLFAEWNDHFRDAARRFWLHYDLPLGAFAGRFAASSDVFKRNGRLPSAAINLVTAHDGFTLRDCVCFNHKHNEANGEENRDGTNNNYSNNHGKEGLGGTLDLVERRRDSIHALLTTLLLSQGTPMLLAGDEHGHSQRGNNNAYCQDNQLTWLDWSQASSGLTAFTAALIHLRKRIPALMENRWWEEGDGNVRWLNRYAQPLSTDEWQNGPKQLQILLSDRFLIAINATLEVTEIVLPAGEWHAIPPFAGEDNPVITAVWQGPAHGLCVFQR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias465-479Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000243
EMBL· GenBank· DDBJ
ABE09369.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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