fabG

UniProt ID: Q88LL6
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

FabG is the canonical NADPH-dependent 3-oxoacyl-ACP reductase of Pseudomonas putida KT2440 type-II fatty-acid synthesis. It performs the first reductive step of each elongation round, converting a 3-oxoacyl-ACP to the corresponding (3R)-hydroxyacyl-ACP.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
IEA
GO_REF:0000120
ACCEPT
Summary: Exact core molecular function for FabG.
Reason: UniProt records the NADPH-dependent beta-ketoacyl-ACP reduction.
Supporting Evidence:
file:PSEPK/fabG/fabG-uniprot.txt
Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP
file:PSEPK/fabG/fabG-deep-research-openscientist.md
Its primary function is to catalyze the NADPH-dependent reduction of 3-oxoacyl-ACP (Ξ²-ketoacyl-ACP) to (3R)-3-hydroxyacyl-ACP.
GO:0006633 fatty acid biosynthetic process
IEA
GO_REF:0000120
ACCEPT
Summary: Correct core pathway assignment.
Reason: UniProt places FabG in fatty-acid biosynthesis.
Supporting Evidence:
file:PSEPK/fabG/fabG-uniprot.txt
PATHWAY: Lipid metabolism; fatty acid biosynthesis.
GO:0030497 fatty acid elongation
IEA
GO_REF:0000117
ACCEPT
Summary: Correct specific process assignment for the iterative FabG step.
Reason: UniProt identifies this as the first reductive step in the elongation cycle.
Supporting Evidence:
file:PSEPK/fabG/fabG-uniprot.txt
in the elongation cycle of fatty acid biosynthesis.
GO:0051287 NAD binding
IEA
GO_REF:0000120
MODIFY
Summary: Cofactor class is incorrect for the NADPH-dependent target enzyme.
Reason: FabG uses NADPH/NADP+, so NADP binding is the appropriate cofactor term.
Proposed replacements: NADP binding
Supporting Evidence:
file:PSEPK/fabG/fabG-uniprot.txt
Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP

Core Functions

NADPH-dependent reduction of 3-oxoacyl-ACP to (3R)-hydroxyacyl-ACP during each FAS-II elongation round.

Supporting Evidence:
  • file:PSEPK/fabG/fabG-uniprot.txt
    Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP
  • file:PSEPK/fabG/fabG-deep-research-openscientist.md
    Its primary function is to catalyze the NADPH-dependent reduction of 3-oxoacyl-ACP (Ξ²-ketoacyl-ACP) to (3R)-3-hydroxyacyl-ACP.

References

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Suggested Questions for Experts

Q: Can any KT2440 reductase compensate for FabG loss during core fatty-acid synthesis?

Suggested Experiments

Experiment: Compare fabG depletion with PP_0581 overexpression using acyl-ACP profiling and growth rescue to test functional redundancy.

Deep Research

OpenScientist

(fabG-deep-research-openscientist.md)

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πŸ“š Additional Documentation

Notes

(fabG-notes.md)

fabG curation notes

  • UniProt accession Q88LL6 identifies the NADPH-dependent reduction of
    beta-ketoacyl-ACP in the fatty-acid elongation cycle
    [file:PSEPK/fabG/fabG-uniprot.txt,
    "Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP"].
  • The exact FabG molecular function, fatty-acid elongation, and fatty-acid
    biosynthesis annotations are accepted.
  • Generic NAD binding is replaced by NADP binding because the recorded
    reaction uses NADPH/NADP+.

πŸ“„ View Raw YAML

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