lpxC

UniProt ID: P47205
Organism: Pseudomonas aeruginosa PAO1
Review Status: COMPLETE
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Gene Description

LpxC (PA4406, EnvA) is the zinc-dependent UDP-3-O-[(R)-3-hydroxyacyl]-N-acetylglucosamine deacetylase of Pseudomonas aeruginosa. It removes the acetyl group from UDP-3-O-acyl-GlcNAc, the second and committed step of lipid A (Raetz pathway) biosynthesis, and so is required for lipopolysaccharide and outer membrane synthesis. The recombinant enzyme is soluble, sensitive to EDTA and reactivated by divalent metal. LpxC is essential and a major target of antibacterial inhibitor development.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0005737 cytoplasm
IBA
GO_REF:0000033
ACCEPT
Summary: IBA cytoplasm from PTN002134692, seeded by E. coli LpxC and Arabidopsis LpxC.
Reason: LpxC is a soluble cytoplasmic enzyme in bacteria, consistent with its expression as a soluble protein; the mitochondrial location of the plant seeds does not apply here.
Supporting Evidence:
PMID:9068651
this construct yielded active protein to approximately 18% of the soluble fraction
GO:0009245 lipid A biosynthetic process
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from PTN002134692, seeded by E. coli LpxC (P0A725) and this gene.
Reason: LpxC catalyses the committed step of lipid A biosynthesis; the IBD stands on E. coli LpxC.
Supporting Evidence:
file:PSEAE/lpxC/lpxC-uniprot.txt
the committed step in lipid A biosynthesis
GO:0009245 lipid A biosynthetic process
IDA
PMID:9068651
Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc...
ACCEPT
Summary: PseudoCAP IDA seed of PTN002134692.
Reason: The paper assayed and purified the deacetylase that performs the committed step of lipid A biosynthesis; seed verdict SOUND.
Supporting Evidence:
file:PSEAE/lpxC/lpxC-uniprot.txt
the committed step in lipid A biosynthesis
PMID:9068651
this construct yielded active protein to approximately 18% of the soluble fraction
GO:0009245 lipid A biosynthetic process
IEA
GO_REF:0000120
ACCEPT
Summary: UniRule mapping.
Reason: As for the IBA row.
Supporting Evidence:
file:PSEAE/lpxC/lpxC-uniprot.txt
the committed step in lipid A biosynthesis
GO:0103117 UDP-3-O-acyl-N-acetylglucosamine deacetylase activity
EXP
PMID:9068651
Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc...
ACCEPT
Summary: UniProt EXP from the purified recombinant enzyme.
Reason: Core activity.
Supporting Evidence:
file:PSEAE/lpxC/lpxC-uniprot.txt
the committed step in lipid A biosynthesis
PMID:9068651
this construct yielded active protein to approximately 18% of the soluble fraction
GO:0103117 UDP-3-O-acyl-N-acetylglucosamine deacetylase activity
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from PTN002134692 (E. coli, Aquifex, Arabidopsis and this gene).
Reason: Core activity, conserved in the family.
Supporting Evidence:
file:PSEAE/lpxC/lpxC-uniprot.txt
the committed step in lipid A biosynthesis
GO:0103117 UDP-3-O-acyl-N-acetylglucosamine deacetylase activity
IEA
GO_REF:0000120
ACCEPT
Summary: UniRule mapping.
Reason: Core activity.
Supporting Evidence:
file:PSEAE/lpxC/lpxC-uniprot.txt
the committed step in lipid A biosynthesis

Core Functions

Zinc-dependent deacetylation of UDP-3-O-acyl-GlcNAc, the committed step of lipid A biosynthesis.

Supporting Evidence:
  • file:PSEAE/lpxC/lpxC-uniprot.txt
    the committed step in lipid A biosynthesis
  • PMID:9068651
    this construct yielded active protein to approximately 18% of the soluble fraction

References

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Notes

(lpxC-notes.md)

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