fadA

UniProt ID: Q88L01
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

fadA encodes the beta subunit of the cytoplasmic FadBA fatty acid oxidation complex. Its 3-ketoacyl-CoA thiolase activity cleaves a beta-oxidation intermediate with coenzyme A to release acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0003988 acetyl-CoA C-acyltransferase activity
IEA
GO_REF:0000120
ACCEPT
Summary: FadA catalyzes the reversible thiolase reaction used in the cleavage direction during fatty acid beta-oxidation.
Reason: The reviewed UniProt entry assigns EC 2.3.1.16 and Rhea 21564 to FadA.
Supporting Evidence:
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
Reaction=an acyl-CoA + acetyl-CoA = a 3-oxoacyl-CoA + CoA;
GO:0005737 cytoplasm
IEA
GO_REF:0000120
ACCEPT
Summary: FadA is annotated as cytoplasmic by the reviewed UniProt entry.
Reason: The localization is explicitly assigned by the FadA HAMAP rule.
Supporting Evidence:
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
SUBCELLULAR LOCATION: Cytoplasm
GO:0006631 fatty acid metabolic process
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: This broad process is true but less informative than fatty acid beta-oxidation.
Reason: Retain the specific beta-oxidation process annotation.
Supporting Evidence:
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
GO:0006635 fatty acid beta-oxidation
IEA
GO_REF:0000120
ACCEPT
Summary: FadA catalyzes the final thiolytic step of each beta-oxidation turn.
Reason: UniProt explicitly describes both the pathway and the two-carbon-shortening reaction.
Supporting Evidence:
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
Catalyzes the final step of fatty acid oxidation in which
GO:0010124 phenylacetate catabolic process
IEA
GO_REF:0000118
REMOVE
Summary: The reviewed FadA record supports fatty acid beta-oxidation, not phenylacetate catabolism.
Reason: KT2440 catabolizes phenylacetate through a dedicated paa operon whose thiolase step is already filled by paaJ (Q88HS3, PP_3280, EC 2.3.1.174), with the flanking steps covered by paaH (Q88HS1, PP_3282) and paaF (Q88HR9, PP_3284), while Q88L01 is assigned to the FadA-specific PANTHER subfamily PTHR43853:SF11 and typed by HAMAP rule MF_01620, both of which confine it to fatty acid beta-oxidation. The term is an unreviewed TreeGrafter inference (GO_REF:0000118, WITH/FROM PANTHER:PTN002466592) and reaches this entry by thiolase-fold propagation rather than by any FadA-specific role. That paaJ receives GO:0010124 from a different node (PANTHER:PTN001291485) corroborates this but is not decisive on its own, since two thiolase clades could in principle both act in the pathway. Note that PTN002466592 is also among the sources of the GO:0006635 annotation accepted above, there joined by UniRule:UR000080052 and UniPathway:UPA00659: the node is a beta-oxidation node, and it is the phenylacetate term sitting on it that is anomalous, so this REMOVE does not undercut that ACCEPT.
Supporting Evidence:
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
PANTHER; PTHR43853:SF11; 3-KETOACYL-COA THIOLASE FADA; 1.
file:PSEPK/fadA__Q88L01/fadA__Q88L01-goa.tsv
GO:0010124 phenylacetate catabolic process biological_process ECO:0007826 IEA GO_REF:0000118 PANTHER:PTN002466592
file:PSEPK/paaJ/paaJ-goa.tsv
GO:0010124 phenylacetate catabolic process biological_process ECO:0007826 IEA GO_REF:0000118 PANTHER:PTN001291485
file:PSEPK/fadA__Q88L01/fadA__Q88L01-notes.md
paaJ receives GO:0010124 from a different TreeGrafter node
file:PSEPK/fadA__Q88L01/fadA__Q88L01-notes.md
KT2440 runs phenylacetate catabolism through a dedicated
GO:0016042 lipid catabolic process
IEA
GO_REF:0000120
MARK AS OVER ANNOTATED
Summary: Lipid catabolic process is a broad parent of the supported fatty acid beta-oxidation role.
Reason: Retain the more specific process annotation.
Supporting Evidence:
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
GO:0016746 acyltransferase activity
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: This generic transferase parent is less informative than acetyl-CoA C-acyltransferase activity.
Reason: Retain GO:0003988 as the specific catalytic function.
Supporting Evidence:
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
EC=2.3.1.16
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: This acyltransferase parent is correct but less informative than the specific thiolase activity.
Reason: Retain GO:0003988 as the specific catalytic function.
Supporting Evidence:
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
EC=2.3.1.16
GO:0036125 fatty acid beta-oxidation multienzyme complex
IEA
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
NEW
Summary: FadA is the beta subunit of a heterotetrameric FadBA fatty acid beta-oxidation complex.
Reason: The reviewed UniProt entry explicitly places FadA in a heterotetramer with FadB, but this complex annotation is absent from the current GOA set.
Supporting Evidence:
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
Heterotetramer of two alpha chains (FadB) and two beta chains

Core Functions

FadA catalyzes thiolytic cleavage of 3-oxoacyl-CoA to acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms in the FadBA complex.

Supporting Evidence:
  • file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
    Catalyzes the final step of fatty acid oxidation in which
  • file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
    Heterotetramer of two alpha chains (FadB) and two beta chains

References

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Suggested Questions for Experts

Q: Which chain lengths are preferentially processed by the FadBA complex relative to other KT2440 thiolase paralogs?

Suggested experts: Pseudomonas fatty acid metabolism experts

Suggested Experiments

Experiment: Compare fatty-acid growth and acyl-CoA intermediate profiles for fadA and pathway-specific thiolase deletions, with complementation by Q88L01.

Type: comparative genetics and targeted acyl-CoA metabolomics

πŸ“š Additional Documentation

Notes

(fadA__Q88L01-notes.md)

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