F0M1N2 · F0M1N2_PSEPM

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.

Catalytic activity

Features

Showing features for binding site, active site, site.

168050100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site269alpha-maltose 1-phosphate (UniProtKB | ChEBI)
Binding site329alpha-maltose 1-phosphate (UniProtKB | ChEBI)
Binding site364alpha-maltose 1-phosphate (UniProtKB | ChEBI)
Active site399Nucleophile
Binding site400alpha-maltose 1-phosphate (UniProtKB | ChEBI)
Active site428Proton donor
Site485Transition state stabilizer
Binding site538-539alpha-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
    • Ordered locus names
      Asphe3_07750

Organism names

Accessions

  • Primary accession
    F0M1N2

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain211-567Glycosyl hydrolase family 13 catalytic

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    680
  • Mass (Da)
    75,522
  • Last updated
    2011-05-03 v1
  • MD5 Checksum
    89BE13888A43E5D586F763B35F7D4AD0
MSKGHITDGLRFGRFPITAVQPVVEGGKFPAKALPGEGIVVGATAFREGHDQLGVSAVLFDPDGNERQRVRLAPPRGERGMGTDRWEGVLTPSDTGNWSFAIEAWHDRYGTWHHNAEVKVEAGIDVELMLAEGSALLGEAAEDESRSEWDRGVLRAAAGRLADTSLSTEERLGAGFGHDVAGVVGHQPIRELVTVSEKFPLNVERDRAGRGAWYEFFPRSEGAVKDHATGAWTSGNFRTAAKRLDAVAAMGFDVIYMPPIHPIGVQHRKGPNNTLIAGPNDPGSPWAIGAAEGGHDAIHPDLGTFEDFDAFVARANELGLEVALDLALQAAPDHPWVQSHPEWFTTRVDGSIAYAENPPKKYQDIYPLNFDNDPEGLSNEILRIVLLWVSHGVKIFRVDNPHTKPVWFWEWLIAQVNKEVPGVVFLAEAFTRPAMMHALGRAGFQQSYTYFTWRNTKKEIESYFNEVSHESAAFFRPNFFVNTPDILTEYLQFGGPAAFRIRAALAATASPLWGVYAGYELYEHVARPGAEEYIDNEKFEYKERDWDAAAHSGRTLAPYITRLNEIRHAHPALQDLQNLTVHHSTDEATVVYSKHKTLPDGSKDTLIVVVNVDPHATRECTVSLDLAALELDPQDLTHNGGFHVEDLISGESWEWGEYNYVRLDPHVEPAHILSVRRTHQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002379
EMBL· GenBank· DDBJ
ADX71978.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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