pgm

UniProt ID: Q88GY7
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
Aliases:
PP_3578
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Gene Description

pgm (PP_3578) encodes an alpha-D-phosphohexomutase family phosphoglucomutase. It catalyzes the reversible conversion of alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, linking central hexose-phosphate metabolism with nucleotide-sugar and storage/carbohydrate biosynthetic pools.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000287 magnesium ion binding
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: magnesium ion binding is biologically plausible for this enzyme but is ancillary to the more specific catalytic function.
Reason: Retain as a supporting/non-core annotation rather than using it as the main functional summary.
GO:0004614 phosphoglucomutase activity
IEA
GO_REF:0000120
ACCEPT
Summary: phosphoglucomutase activity is consistent with the curated UniProt name, EC/family evidence, and the gene product role summarized here.
Reason: This is a specific, biologically appropriate annotation for this gene product.
GO:0005975 carbohydrate metabolic process
IEA
GO_REF:0000120
ACCEPT
Summary: carbohydrate metabolic process is consistent with the curated UniProt name, EC/family evidence, and the gene product role summarized here.
Reason: This is a specific, biologically appropriate annotation for this gene product.
GO:0006166 purine ribonucleoside salvage
IEA
GO_REF:0000118
MARK AS OVER ANNOTATED
Summary: This TreeGrafter process is coupled to a propagated phosphopentomutase assignment, whereas Q88GY7 is specifically classified as an EC 5.4.2.2 phosphoglucomutase in a phosphoglucomutase subfamily.
Reason: The broad family contains divergent phosphomutases, but no target-specific evidence connects Q88GY7 to purine ribonucleoside salvage.
Supporting Evidence:
file:PSEPK/pgm/pgm-uniprot.txt
DE EC=5.4.2.2 {ECO:0000256|NCBIfam:TIGR01132};
GO:0008973 phosphopentomutase activity
IEA
GO_REF:0000118
MARK AS OVER ANNOTATED
Summary: This TreeGrafter assignment appears propagated across divergent phosphomutase functions; Q88GY7 is specifically classified as a phosphoglucomutase and lacks target-specific phosphopentomutase evidence.
Reason: Retain the established EC 5.4.2.2 activity without importing a distinct pentose-phosphate salvage reaction from deeper family ancestry.
Supporting Evidence:
file:PSEPK/pgm/pgm-uniprot.txt
DR InterPro; IPR005852; PGM_a-D-Glc-sp.
GO:0016868 intramolecular phosphotransferase activity
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: intramolecular phosphotransferase activity is biologically plausible for this enzyme but is ancillary to the more specific catalytic function.
Reason: Retain as a supporting/non-core annotation rather than using it as the main functional summary.
GO:0006011 UDP-alpha-D-glucose metabolic process
ISS
file:PSEPK/pgm/pgm-deep-research-openscientist.md
NEW
Summary: Pgm supplies glucose 1-phosphate at the branch point leading to UDP-alpha-D-glucose and downstream nucleotide-sugar-dependent glycans.
Supporting Evidence:
file:PSEPK/pgm/pgm-deep-research-openscientist.md
it functions at the **G1P/G6P branch point** that couples Entner-Doudoroff central carbon metabolism to nucleotide-sugar-dependent biosynthesis (UDP-/ADP-glucose for glycogen, trehalose, LPS/O-antigen, exopolysaccharides, and dTDP-L-rhamnose)

Core Functions

phosphoglucomutase activity supporting the Phosphoglucomutase (EC 5.4.2.2) role summarized for pgm.

Supporting Evidence:
  • file:PSEPK/pgm/pgm-uniprot.txt
    DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-UniRule.

References

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Suggested Questions for Experts

Q: How is glucose 1-phosphate flux divided between Pgm and the bifunctional AlgC enzyme under nucleotide-sugar and storage-polymer demand?

Suggested Experiments

Experiment: Measure glucose- and mannose-phosphate mutase kinetics for purified Pgm and quantify pathway flux in pgm and algC perturbation strains.

Type: comparative enzymology and metabolic flux analysis

Deep Research

Asta

(pgm-deep-research-asta.md)

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OpenScientist

(pgm-deep-research-openscientist.md)

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