glmM

UniProt ID: Q9HV50
Organism: Pseudomonas aeruginosa PAO1
Review Status: COMPLETE
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Gene Description

GlmM (PA4749) is the phosphoglucosamine mutase of Pseudomonas aeruginosa, a member of the alpha-D-phosphohexomutase superfamily. It converts glucosamine-6-phosphate to glucosamine-1-phosphate, the second step of the hexosamine branch leading to UDP-N-acetylglucosamine, the common precursor of peptidoglycan and lipopolysaccharide. The P. aeruginosa gene complements an E. coli glmM mutant, restoring peptidoglycan synthesis and growth, and the purified His-tagged enzyme has phosphoglucosamine mutase activity similar to the E. coli enzyme. It also shows phosphomannomutase (about 20 percent) and phosphoglucomutase (about 2 percent) side activities, but it cannot replace the dedicated bifunctional PMM/PGM AlgC in alginate synthesis. Like other phosphohexomutases it is expected to use a phosphoserine catalytic intermediate and Mg2+.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000287 magnesium ion binding
IEA
GO_REF:0000120
ACCEPT
Summary: UniRule/InterPro mapping; phosphohexomutases use Mg2+ bound at the catalytic phosphoserine site.
Reason: Family-wide cofactor (HAMAP GlmM rule); not assayed in this paper but consistent with the superfamily.
Supporting Evidence:
PMID:10913078
The product of this gene is here identified as the phosphoglucosamine mutase (GlmM) which catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate
GO:0004614 phosphoglucomutase activity
IDA
PMID:10913078
Identification of the Pseudomonas aeruginosa glmM gene, enco...
MARK AS OVER ANNOTATED
Summary: PseudoCAP IDA row: PGM activity is about 2 percent of the GlmM activity of the purified enzyme.
Reason: Real but low in vitro side activity of unknown physiological relevance; the dedicated PGM/PMM AlgC exists and GlmM does not substitute for it. Not removed because it was measured on purified enzyme. Not a PAINT seed.
Supporting Evidence:
PMID:10913078
Beside its phosphoglucosamine mutase activity, the P. aeruginosa enzyme is shown to exhibit phosphomannomutase and phosphoglucomutase activities, which represent about 20 and 2% of its GlmM activity, respectively.
PMID:10913078
when plasmid pIT352 was introduced by triparental mating into the algC mutant strain P. aeruginosa 8858, alginate synthesis was not restored
GO:0004614 phosphoglucomutase activity
IEA
GO_REF:0000117
MARK AS OVER ANNOTATED
Summary: ARBA prediction of PGM activity.
Reason: As for the IDA row: a 2 percent side activity, not the evolved function.
Supporting Evidence:
PMID:10913078
Beside its phosphoglucosamine mutase activity, the P. aeruginosa enzyme is shown to exhibit phosphomannomutase and phosphoglucomutase activities, which represent about 20 and 2% of its GlmM activity, respectively.
GO:0004615 phosphomannomutase activity
IBA
GO_REF:0000033
KEEP AS NON CORE
Summary: IBA from the deep phosphohexomutase node PTN001096974 (136 leaves), seeded by T. kodakarensis PGM/PMM Q68BJ6 and by this gene's PseudoCAP IDA row (self-seed).
Reason: GlmM has a genuine, conserved PMM side activity (20 percent, also seen for E. coli GlmM), so the transfer is not false, but PMM is not GlmM's evolved function; AlgC is the P. aeruginosa PMM. The node also contains bona fide PMMs (ManB, RfbK, Pmm) so the node term suits the clade.
Supporting Evidence:
PMID:10913078
Beside its phosphoglucosamine mutase activity, the P. aeruginosa enzyme is shown to exhibit phosphomannomutase and phosphoglucomutase activities, which represent about 20 and 2% of its GlmM activity, respectively.
PMID:10913078
GlmM enzymes from P. aeruginosa and E. coli exhibit additional PMM (relatively high) and PGM (low) activities
GO:0004615 phosphomannomutase activity
IDA
PMID:10913078
Identification of the Pseudomonas aeruginosa glmM gene, enco...
KEEP AS NON CORE
Summary: PseudoCAP IDA seed of PTN001096974: purified GlmM shows PMM activity at 20 percent of its GlmM activity.
Reason: Seed SOUND as a measurement (full text read): the activity was assayed on purified enzyme. It is a secondary activity; GlmM does not restore alginate synthesis in an algC mutant.
Supporting Evidence:
PMID:10913078
Beside its phosphoglucosamine mutase activity, the P. aeruginosa enzyme is shown to exhibit phosphomannomutase and phosphoglucomutase activities, which represent about 20 and 2% of its GlmM activity, respectively.
PMID:10913078
when plasmid pIT352 was introduced by triparental mating into the algC mutant strain P. aeruginosa 8858, alginate synthesis was not restored
GO:0004615 phosphomannomutase activity
IEA
GO_REF:0000117
KEEP AS NON CORE
Summary: ARBA prediction of PMM activity.
Reason: Consistent with the IDA and IBA rows.
Supporting Evidence:
PMID:10913078
Beside its phosphoglucosamine mutase activity, the P. aeruginosa enzyme is shown to exhibit phosphomannomutase and phosphoglucomutase activities, which represent about 20 and 2% of its GlmM activity, respectively.
GO:0005829 cytosol
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from PTN000501735 seeded by E. coli GlmM.
Reason: Soluble cytoplasmic enzyme; overproduced P. aeruginosa GlmM is mostly soluble.
Supporting Evidence:
PMID:10913078
most of it (about 90%) was recovered in the soluble fraction
GO:0005975 carbohydrate metabolic process
IEA
GO_REF:0000002
MODIFY
Summary: InterPro phosphohexomutase mapping to carbohydrate metabolic process.
Reason: Correct but general; the specific process is GO:0006048 UDP-N-acetylglucosamine biosynthetic process, accepted here (GO:0006048 is not an is_a descendant of GO:0005975, so MODIFY rather than TOO_GENERAL).
Supporting Evidence:
PMID:10913078
the first step in the biosynthetic pathway leading to the formation of UDP- N -acetylglucosamine
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from PTN000501735 seeded by E. coli GlmM.
Reason: GlcN-6-P to GlcN-1-P is a step of UDP-GlcNAc synthesis; supported by this gene's activity data.
Supporting Evidence:
PMID:10913078
The product of this gene is here identified as the phosphoglucosamine mutase (GlmM) which catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate
PMID:10913078
the first step in the biosynthetic pathway leading to the formation of UDP- N -acetylglucosamine
GO:0008966 phosphoglucosamine mutase activity
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from PTN000501735 seeded by E. coli GlmM and this gene (self-seed).
Reason: Core function; IBD stands on E. coli GlmM.
Supporting Evidence:
PMID:10913078
The product of this gene is here identified as the phosphoglucosamine mutase (GlmM) which catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate
GO:0008966 phosphoglucosamine mutase activity
IDA
PMID:10913078
Identification of the Pseudomonas aeruginosa glmM gene, enco...
ACCEPT
Summary: PseudoCAP IDA seed of PTN000501735: purified enzyme has phosphoglucosamine mutase activity.
Reason: Seed SOUND (full text read). Core molecular function.
Supporting Evidence:
PMID:10913078
The product of this gene is here identified as the phosphoglucosamine mutase (GlmM) which catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate
PMID:10913078
shown to restore normal peptidoglycan biosynthesis and cell growth of a glmM Escherichia coli mutant strain
GO:0008966 phosphoglucosamine mutase activity
IEA
GO_REF:0000120
ACCEPT
Summary: UniRule/EC/Rhea mapping; agrees with the IDA.
Reason: Same claim as the IDA row.
Supporting Evidence:
PMID:10913078
The product of this gene is here identified as the phosphoglucosamine mutase (GlmM) which catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate
GO:0009252 peptidoglycan biosynthetic process
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from PTN000501735 seeded by E. coli GlmM and this gene.
Reason: GlmM supplies a step of the peptidoglycan precursor pathway; IBD stands on E. coli GlmM.
Supporting Evidence:
PMID:10913078
shown to restore normal peptidoglycan biosynthesis and cell growth of a glmM Escherichia coli mutant strain
GO:0009252 peptidoglycan biosynthetic process
IDA
PMID:10913078
Identification of the Pseudomonas aeruginosa glmM gene, enco...
ACCEPT
Summary: PseudoCAP IDA seed of PTN000501735: the gene restores peptidoglycan synthesis in an E. coli glmM mutant (strictly complementation, nearer IGI than IDA).
Reason: Seed SOUND (full text read): the enzyme catalyses a step of the precursor pathway, so it takes part in the process.
Supporting Evidence:
PMID:10913078
shown to restore normal peptidoglycan biosynthesis and cell growth of a glmM Escherichia coli mutant strain
GO:0009252 peptidoglycan biosynthetic process
IEA
GO_REF:0000117
ACCEPT
Summary: ARBA prediction; agrees with the IDA.
Reason: Same claim as the IDA row.
Supporting Evidence:
PMID:10913078
shown to restore normal peptidoglycan biosynthesis and cell growth of a glmM Escherichia coli mutant strain
GO:0016868 intramolecular phosphotransferase activity
IEA
GO_REF:0000002
TOO GENERAL
Summary: InterPro mapping to intramolecular phosphotransferase activity.
Reason: Entailed by GO:0008966 phosphoglucosamine mutase activity, accepted here.

Core Functions

Phosphoglucosamine mutase converting glucosamine-6-phosphate to glucosamine-1-phosphate for UDP-N-acetylglucosamine and peptidoglycan synthesis.

Supporting Evidence:
  • PMID:10913078
    The product of this gene is here identified as the phosphoglucosamine mutase (GlmM) which catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate
  • PMID:10913078
    shown to restore normal peptidoglycan biosynthesis and cell growth of a glmM Escherichia coli mutant strain

References

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Suggested Questions for Experts

Q: Should the PMM IBD at PTN001096974 sit on a lower node that excludes the bacterial GlmM subclade, given that GlmM's PMM is a side activity? Note that UniProt now assigns the other seed, Q68BJ6, to PANTHER PTHR43771 rather than PTHR42946.

Suggested Experiments

Experiment: Measure kcat/Km of purified GlmM for GlcN-6-P, Man-1-P and Glc-1-P to quantify the side activities, and test glmM overexpression in an algC deletion for LPS core synthesis.

πŸ“š Additional Documentation

Notes

(glmM-notes.md)

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