fabA

UniProt ID: O33877
Organism: Pseudomonas aeruginosa PAO1
Review Status: COMPLETE
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Gene Description

FabA (PA1610) is the beta-hydroxydecanoyl-ACP dehydratase/isomerase of the dissociated type II fatty acid synthase of Pseudomonas aeruginosa, a hot-dog-fold enzyme of the FabA subfamily. It has two activities: it dehydrates (3R)-hydroxyacyl-ACP intermediates to (2E)-enoyl-ACP (EC 4.2.1.59) during each round of elongation, and, uniquely for this subfamily, it isomerises (2E)-decenoyl-ACP to (3Z)-decenoyl-ACP (EC 5.3.3.14), the committed branch point that introduces the cis double bond into unsaturated fatty acids. The cis-3-decenoyl-ACP it makes is then elongated by FabB. fabA is cotranscribed with fabB as the fabAB operon, and fabA mutants are auxotrophic for unsaturated fatty acids. FabA is a soluble cytosolic enzyme.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0005737 cytoplasm
IEA
GO_REF:0000120
TOO GENERAL
Summary: UniProt subcellular-location mapping. True, but GO:0005829 cytosol, accepted above, is part_of cytoplasm and is already asserted here.
Reason: Entailed by the accepted cytosol row.
GO:0005829 cytosol
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from PTN002824827 (bacterial-restricted node, seeded by E. coli FabA) placing the enzyme in the cytosol. The dissociated type II FAS is a soluble cytosolic system.
Reason: Correct location for a soluble type II FAS enzyme and where its activity acts.
GO:0006633 fatty acid biosynthetic process
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from the eight-node PTN008624492 GO:0006633 IBD, which this gene's own PseudoCAP row helped seed (expected self-appearance in WITH/FROM). FabA performs the dehydration step of each elongation round, so it does part of the process.
Reason: Core and directly performed. Not marked too general despite the accepted GO:0006636 descendant - FabA's dehydratase acts on saturated acyl-ACPs too, so the general term covers work the unsaturated-specific term does not.
Supporting Evidence:
PMID:9286984
Chromosomal fabA and fabB mutants were isolated; the mutants were auxotrophic for unsaturated fatty acids.
GO:0006633 fatty acid biosynthetic process
IEA
GO_REF:0000120
ACCEPT
Summary: InterPro/UniPathway mapping of the same process claim as the IBA row.
Reason: Consistent with the accepted IBA row.
GO:0006636 unsaturated fatty acid biosynthetic process
IEA
GO_REF:0000104
ACCEPT
Summary: UniRule mapping of the unsaturated fatty acid biosynthetic process, matching the PseudoCAP IMP row.
Reason: Core process - FabA's isomerase activity commits carbon to the unsaturated branch.
GO:0006636 unsaturated fatty acid biosynthetic process
IMP
PMID:9286984
Fatty acid biosynthesis in Pseudomonas aeruginosa: cloning a...
ACCEPT
Summary: PseudoCAP row and the seed of the GO:0006633 IBD at PTN008624492. The evidence is the unsaturated-fatty-acid auxotrophy of chromosomal fabA mutants, but for fabA phenotype and catalysis coincide: FabA's isomerase makes the cis-3-decenoyl-ACP intermediate, the committed step of UFA synthesis. This is participation, not mere necessity.
Reason: Core process, performed by this enzyme's own isomerase step. The seeded node term is the parent GO:0006633, so the specific term stays on the gene.
Supporting Evidence:
PMID:9286984
Chromosomal fabA and fabB mutants were isolated; the mutants were auxotrophic for unsaturated fatty acids.
GO:0019171 (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity
IBA
GO_REF:0000033
ACCEPT
Summary: IBA from the PTN008624492 IBD (FabA/FabZ dehydratase node, seeded by E. coli FabA P0A6Q3, E. coli FabZ P0A6Q6 and an Arabidopsis homolog). The (3R)-hydroxyacyl-ACP dehydratase activity is the family-defining activity and is directly supported for PAO1 FabA by its UniProt-curated catalytic activities.
Reason: Sound node assertion at the right level; core activity of the enzyme.
Supporting Evidence:
file:PSEAE/fabA/fabA-uniprot.txt
Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
GO:0019171 (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity
IEA
GO_REF:0000120
ACCEPT
Summary: InterPro/RHEA/EC 4.2.1.59 mapping of the same dehydratase activity, agreeing with the IBA row and the UniProt catalytic activity.
Reason: Consistent electronic assertion of the demonstrated activity.
GO:0034017 trans-2-decenoyl-acyl-carrier-protein isomerase activity
IEA
GO_REF:0000120
ACCEPT
Summary: RHEA/EC 5.3.3.14 mapping of the trans-2-decenoyl-ACP isomerase activity, the UFA-committing activity of the FabA subfamily.
Reason: Core activity; UniProt curates this reaction for the enzyme and it is the step that introduces cis unsaturation.
Supporting Evidence:
file:PSEAE/fabA/fabA-uniprot.txt
Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP];

Core Functions

(3R)-hydroxyacyl-ACP dehydratase of type II fatty acid synthesis: removes water from the beta-hydroxyacyl-ACP intermediate to give the (2E)-enoyl-ACP in each elongation cycle.

Supporting Evidence:
  • file:PSEAE/fabA/fabA-uniprot.txt
    Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;

trans-2-decenoyl-ACP isomerase activity: converts (2E)-decenoyl-ACP to (3Z)-decenoyl-ACP, the committed step that introduces the cis double bond and commits carbon to the unsaturated fatty acid branch.

Supporting Evidence:
  • file:PSEAE/fabA/fabA-uniprot.txt
    Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP];

References

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Suggested Questions for Experts

Q: Over what range of acyl chain lengths does P. aeruginosa FabA act as a dehydratase versus an isomerase, and how is the partition with FabZ (if present) organised in this organism?

Suggested Experiments

Experiment: Assay purified PAO1 FabA for dehydratase and isomerase activities on a graded set of (3R)-hydroxyacyl-ACP and (2E)-enoyl-ACP substrates to define the chain-length dependence of each activity.

πŸ“š Additional Documentation

Notes

(fabA-notes.md)

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