glgE

UniProt ID: Q88FM9
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

GlgE (PP_4060) is a predicted maltosyltransferase that uses alpha-maltose 1-phosphate to extend alpha-1,4-glucan acceptors by two glucosyl residues, releasing phosphate. It is the polymer-elongating enzyme of a trehalose-derived branched alpha-glucan biosynthetic route with TreSB and GlgB.

Proposed New Ontology Terms

alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase activity

Definition: Catalysis of the transfer of a maltosyl group from alpha-maltose 1-phosphate to the nonreducing end of an alpha-1,4-glucan, extending the acceptor by two glucosyl residues and releasing phosphate.

Justification: The exact EC 2.4.99.16/RHEA:42692 reaction transfers a maltosyl disaccharide, which is not represented precisely by the existing hexosyltransferase term.

Parent term: glycosyltransferase activity

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
IEA
GO_REF:0000002
REMOVE
Summary: The GH13 fold mapping assigns hydrolysis, but the supported GlgE reaction transfers maltosyl units from maltose 1-phosphate to glucan.
Reason: The net EC 2.4.99.16/RHEA:42692 reaction is a glycosyl transfer that releases phosphate, not hydrolysis of an O-glycosyl compound. This is a fold-level InterPro overextension and should not be propagated.
Supporting Evidence:
file:PSEPK/glgE/glgE-uniprot.txt
Reaction=alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl](n) =
GO:0005975 carbohydrate metabolic process
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: GlgE directly transforms carbohydrate substrates in alpha-glucan synthesis.
Reason: This broad process is correct but adds little beyond the accepted alpha-glucan biosynthetic process and does not identify the reaction.
Supporting Evidence:
file:PSEPK/glgE/glgE-uniprot.txt
involved in a branched alpha-glucan biosynthetic pathway
GO:0016757 glycosyltransferase activity
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: GlgE is a glycosyltransferase, but this term is broader than its hexosyl transfer.
Reason: The annotation has the correct reaction class but is redundant with the more informative GO:0016758 annotation.
Supporting Evidence:
file:PSEPK/glgE/glgE-uniprot.txt
Maltosyltransferase that uses maltose 1-phosphate (M1P)
GO:0016758 hexosyltransferase activity
IEA
GO_REF:0000104
ACCEPT
Summary: GlgE transfers a maltosyl unit from maltose 1-phosphate to alpha-1,4-glucan.
Reason: The HAMAP assignment specifies EC 2.4.99.16/RHEA:42692, GlgE-specific InterPro signatures, and binding sites for alpha-maltose 1-phosphate. GO lacks a substrate-specific GlgE molecular-function term. GO:0016758 is the most specific available annotation, although the reaction transfers a maltosyl disaccharide rather than a single hexosyl group.
Supporting Evidence:
file:PSEPK/glgE/glgE-uniprot.txt
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProtKB-UniRule.
file:PSEPK/glgE/glgE-uniprot.txt
DR InterPro; IPR026585; GlgE.
GO:0030979 alpha-glucan biosynthetic process
IEA
GO_REF:0000104
ACCEPT
Summary: GlgE elongates alpha-1,4-glucan using maltose 1-phosphate.
Reason: Polymer extension is a direct alpha-glucan biosynthetic reaction. This does not assign GlgE the TreSB precursor-generating or GlgB branching reactions.
Supporting Evidence:
file:PSEPK/glgE/glgE-uniprot.txt
the sugar donor to elongate linear or branched alpha-(1->4)-glucans.

Core Functions

Transfers maltosyl units from alpha-maltose 1-phosphate to the nonreducing end of alpha-1,4-glucan, extending the polymer by two glucosyl residues and releasing phosphate.

Supporting Evidence:
  • file:PSEPK/glgE/glgE-uniprot.txt
    Reaction=alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl](n) =
  • file:PSEPK/glgE/glgE-deep-research-openscientist.md
    **GlgE (Q88FM9, locus PP_4060) is Ξ±-maltose-1-phosphate:(1β†’4)-Ξ±-D-glucan 4-Ξ±-D-maltosyltransferase (GMPMT; EC 2.4.99.16), a cytoplasmic glycoside-hydrolase family 13 (GH13_3) enzyme.**
  • PMID:24689960
    It catalyzes the Ξ±-retaining transfer of maltosyl units from Ξ±-maltose 1-phosphate to maltooligosaccharides and is predicted to use a double-displacement mechanism.

References

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Deep Research

OpenScientist

(glgE-deep-research-openscientist.md)

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πŸ“š Additional Documentation

Notes

(glgE-notes.md)

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