A0A6C1SPT9 · A0A6C1SPT9_9PROT

  • Protein
    Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
  • Gene
    glgE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.

Caution

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

Catalytic activity

Features

Showing features for binding site, active site, site.

170050100150200250300350400450500550600650700
TypeIDPosition(s)Description
Binding site295alpha-maltose 1-phosphate (UniProtKB | ChEBI)
Binding site355alpha-maltose 1-phosphate (UniProtKB | ChEBI)
Binding site390alpha-maltose 1-phosphate (UniProtKB | ChEBI)
Active site426Nucleophile
Binding site427alpha-maltose 1-phosphate (UniProtKB | ChEBI)
Active site455Proton donor
Site513Transition state stabilizer
Binding site566-567alpha-maltose 1-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionhexosyltransferase activity
Molecular Functionhydrolase activity, hydrolyzing O-glycosyl compounds
Biological Processalpha-glucan biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
  • EC number
  • Short names
    GMPMT
  • Alternative names
    • (1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase

Gene names

    • Name
      glgE
    • ORF names
      EA406_11885

Organism names

Accessions

  • Primary accession
    A0A6C1SPT9

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-38Disordered
Compositional bias21-38Basic and acidic residues
Domain243-591Glycosyl hydrolase family 13 catalytic

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgE subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    700
  • Mass (Da)
    80,571
  • Last updated
    2020-06-17 v1
  • Checksum
    C55A045F90564902
MPPKDEAASPPATPSQPAADDDAAPHRHHKDESARGRAHRLFLPLAEKARSRSIVIQNVQPQVNCGRYPVKREVGDTLHVTAEIFREGHDKLSAVILYRRISESQWRESPMREVNFGLAEWAGSIALYENARYLFTVEAWTDLFASWCDEVEKKLGAGQNVHLELVEGRELVEEAAARAQGDDAKRLQAVLDAFKALDDGARASLLLGQDVRAMMARWPDRSTAIRYDKELEVMVDRLQARYAAWYEMFPRSQGQIPGRSATFADCEARLPEVRRMGFDVVYFVPIHPIGRTFRKGRNNTLNAGPDDPGSPYAIGGPEGGHTAIHPELGTLEDFRRFVAACHAQGMEVALDFAVQCSPDHPWIKDHPEWFLFRADGSIKYAENPPKKYQDIVNVDFYCTDWQSLWEELLFVVNFWVDQGVKIFRVDNPHTKPVPFWEWLIREVQEKHPDVIFLAEAFTRPPMLKMMAKIGFGQSYTYFTWRHGKQELTEYLTELTQTDVKEYLRPNFFTNTPDINPPYLQTGGRPAHQIRLVLAATLSSVYGMYNGFELCEATPIPGKEEYLNSEKYEYKVWDWDQPGNIKDYITRINQIRRDNPALHELDNLRFYPSTSDNILFYGKMTPDRRNMLFIAVNLDPFVANDGFVSFPLEEMGLGPRDRFIAEELFSFRRLEWQGAKHWIRLDPYVNPCEIFRITRIGDVGW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias21-38Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
REES01000111
EMBL· GenBank· DDBJ
TVR96455.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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