A0A371BMT2 · A0A371BMT2_9MICC

  • Protein
    1,4-alpha-glucan branching enzyme GlgB
  • Gene
    glgB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Glycan biosynthesis; glycogen biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site909Nucleophile
Active site962Proton donor

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function1,4-alpha-glucan branching enzyme activity
Molecular Function1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis)
Molecular Functioncation binding
Molecular Functionhydrolase activity, hydrolyzing O-glycosyl compounds
Biological Processglycogen biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    1,4-alpha-glucan branching enzyme GlgB
  • EC number
  • Alternative names
    • 1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase
    • Alpha-(1->4)-glucan branching enzyme
    • Glycogen branching enzyme
      (BE
      )

Gene names

    • Name
      glgB
    • ORF names
      DXK94_17870

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • RT-1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Arthrobacter

Accessions

  • Primary accession
    A0A371BMT2

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias477-495Polar residues
Region477-503Disordered
Domain757-1107Glycosyl hydrolase family 13 catalytic

Sequence similarities

Belongs to the aminoglycoside phosphotransferase family.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,243
  • Mass (Da)
    134,906
  • Last updated
    2018-11-07 v1
  • Checksum
    D6558F9B9ABA75AF
MNQPILTPALTALLKEWLPRQRWFPVKTPDFDMSQAGSLGLDDPSRHAALAVFLLNVTTRGADGGRRTAVVQVPLSFRPAPAAGMERALVGQAAGTDPSRPWVYDAVHDPDFVGGWLELIRQESKAPSGTAMGYKVPGSYRLPTARGVVKVLSGEQSNSSVIVDDGESAAIVKFFRVLSEGTNPEVEVGAALTSAGTSEVPATLGWVRGEWMAQGRTASGDTGTRHVQGELAVAHEFLAGGRDAWRLAVDAARSGTDFTAEARALGAATATVHRRLAEALGQSAESEAGKVIGPGVAQRVRQAWTEAGPAVGPYDEPLNALLDGLDGVPGGPLQRIHGDLHLGQILQVPQAAGTAGGGARWAILDFEGEPMRPIAERNVPDVPLRDVVGMLRSFDYAAGAAQREQEGAHVPASWVDDCADAFLEGYAGVTPGTVDRNSPLFVALWLDKALYEVVYEMRNRPDWLAIPVNASRRLLSGNSSGHQAGAASEGNEMTGSARTDRPGVPLHVDDGILGRIANGEHHAPHSVLGAHLDDYGHVTIRTVKHLAEAVTVITAAGEVPMEHEAHGVWAAVLEPLQQGHVPDYRLSVTYPGAEPVTVDEPYRYLPTVGEVDLHLIGEGRHEKLWEVLGAHVQHYKSSLGDVDGVSFAVWAPNAQAVRLKGDFNGWDGREHSLRSLGSSGVWEIFVPGVLAGACYKFEIRTRSGYWVEKADPLAFGTEVPPLTASKVVEPSYAFKDDEWMEARAQRDPHNSAMSVYEVHLGSWRLGLGYRELAKELVDYVKWLGFTHVEFMPVAEHPFGGSWGYQVTSYFAPTSRFGHPDEFRYLVDTLHQAGIGVLLDWVPAHFPKDSWALAQFDGEALYEHADPNLGEHPDWGTLIFDFGRTEVRNFLVANALYWLDEFHIDGLRVDAVASMLYLDYSRQDGQWQPNRFGGRENLEAISFLQEVNATVYKTHPGAVMIAEESTAFPGVTAPTSHGGLGFGLKWNMGWMHDSLKYASEDPVNRKWHHGTVTFSMVYAFTENFLLPISHDEVVHGKGSMLRKMPGDRWQQLANLRAFLAYQWAHPGKQLIFMGTEFGQEAEWSEQHGLDWWLADIPAHKGLQLLTKDLNELYKSTPALYTRDNEPGGFQWINGGDADRNVLSFIRWDTDGNPLVCAINFSGAPHVGYTLGVPTAGAWTEVLNTDHTTYGGSGVLNDGELKASGEGQDGQPATLTVTLPPLGASYFKPGAAKPSAAKPGAAGTA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias477-495Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QRGQ01000036
EMBL· GenBank· DDBJ
RDV08661.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp