Bacterial fatty acid beta-oxidation spiral

A reusable bacterial four-reaction spiral that shortens a fatty acyl-CoA by two carbon atoms per turn. An acyl-CoA dehydrogenase forms a trans-2-enoyl-CoA, an enoyl-CoA hydratase forms a (3S)-3-hydroxyacyl-CoA, a hydroxyacyl-CoA dehydrogenase forms a 3-oxoacyl-CoA, and a thiolase releases acetyl-CoA plus a chain-shortened acyl-CoA that re-enters the first reaction. Bacterial pathway architecture can use separate enzymes or a multifunctional FadBA complex; free-fatty-acid activation and unsaturated-fatty-acid auxiliary reactions are outside the core spiral.

MODULE:bacterial_fatty_acid_beta_oxidationDRAFTCONCRETEMetabolic Pathwaymodules/bacterial_fatty_acid_beta_oxidation.yaml
fatty acid beta-oxidationGO:0006635
GO:0006635
fatty acid beta-oxidation
Defines the biological process represented by the four-reaction spiral.
file:PSEPK/fadE/fadE-uniprot.txt
PSEPK FadE UniProt record
Q88LN6 is assigned long- and medium-chain acyl-CoA dehydrogenase reactions that reduce electron-transfer flavoprotein during beta oxidation.
file:PSEPK/fadB/fadB-ai-review.yaml
PSEPK fadB gene review
Q88L02 supplies the enoyl-CoA hydratase and (3S)-3-hydroxyacyl-CoA dehydrogenase activities of the FadBA complex.
file:PSEPK/fadA__Q88L01/fadA__Q88L01-uniprot.txt
PSEPK FadA UniProt record
Q88L01 is the thiolase subunit of the FadBA complex and releases acetyl-CoA plus a chain-shortened acyl-CoA in the final reaction.

The module is species-neutral and uses Pseudomonas putida KT2440 as a bacterial realization. FadD-dependent ligation of free fatty acids to CoA is an optional entry process, not a spiral reaction. Enoyl-CoA isomerases, 2,4-dienoyl-CoA reductases, and related enzymes required for unsaturated substrates are auxiliary. Alkane oxidation, phenylacetate degradation, glutaryl-CoA oxidation, PHA metabolism, transport, and specialty acyl-CoA pathways are separate modules. Molecular functions and exact chemistry are asserted only on leaf annotons; no generic cytoplasmic location is asserted at module level.

5Nodes
4Parts
0Variant Sets
0Variants
4Annotons
4Connections

Derived QC

Recommended-field compliance

60.0% recommended fields populated
  • module.knowledge_gaps[0] · status (0/1)
  • module.knowledge_gaps[0] · provenance (0/1)

Module deep research

✗ none found

No MODULE:bacterial_fatty_acid_beta_oxidation deep-research report alongside the module YAML.

Leaf nodes lacking representative members

✓ every leaf node grounds to a representative protein.

Template conformance

✓ every declared conforms_to bundle matches its template motif.

Gene-review completeness (3/3 grounded genes reviewed)

2 complete review(s) · 2 with deep research · 0 missing review · 1 reviewed but lacking deep research

Gene Review Complete Deep research
fadA Q88L01 ✓ ✓ ✗
fadB Q88L02 ✓ ✓ ✓
fadE Q88LN6 ✓ 7/8 ✓

Details

Context
bacteriaNCBITaxon:2
Bacterial fatty acid beta-oxidation spiralMetabolic Pathwaybacterial_fatty_acid_beta_oxidation
fatty acid beta-oxidationGO:0006635
Context
bacteriaNCBITaxon:2

Connections

The trans-2-enoyl-CoA product is hydrated in the second reaction.
The (3S)-3-hydroxyacyl-CoA product is oxidized in the third reaction.
The 3-oxoacyl-CoA product undergoes thiolytic cleavage.
The chain-shortened fatty acyl-CoA re-enters the spiral.
Part 1: FAD-dependent fatty acyl-CoA dehydrogenation
Fatty acyl-CoA to trans-2-enoyl-CoAReactionbacterial_acyl_coa_dehydrogenation

Annotons

Bacterial FadE acyl-CoA dehydrogenase activity
fade_acyl_coa_dehydrogenase_activity
Participant: Family: bacterial FadE acyl-CoA dehydrogenase family
Family:
bacterial FadE acyl-CoA dehydrogenase familyPANTHER:PTHR48083:SF18
Representative Members: FadE (Pseudomonas putida KT2440)UniProtKB:Q88LN6

Function

acyl-CoA dehydrogenase activityGO:0003995
Substrates: fatty acyl-CoA oxidized electron-transfer flavoprotein
Products: trans-2-enoyl-CoA reduced electron-transfer flavoprotein

Processes

fatty acid beta-oxidation using acyl-CoA dehydrogenaseGO:0033539

Introduces the trans double bond and transfers electrons to ETF.

Part 2: trans-2-enoyl-CoA hydration
trans-2-enoyl-CoA to (3S)-3-hydroxyacyl-CoAReactionbacterial_enoyl_coa_hydration

Annotons

Bacterial FadB enoyl-CoA hydratase activity
fadb_enoyl_coa_hydratase_activity
Participant: Family: bacterial FadB family
Family:
bacterial FadB familyInterPro:IPR012799
Representative Members: FadB (Pseudomonas putida KT2440)UniProtKB:Q88L02

Function

enoyl-CoA hydratase activityGO:0004300
Substrates: trans-2-enoyl-CoA water
Products: (3S)-3-hydroxyacyl-CoA

Processes

fatty acid beta-oxidationGO:0006635

The FadB hydratase domain performs the second reaction; in the PSEPK realization FadB acts with FadA in the FadBA complex.

Part 3: NAD-dependent hydroxyacyl-CoA oxidation
(3S)-3-hydroxyacyl-CoA to 3-oxoacyl-CoAReactionbacterial_hydroxyacyl_coa_oxidation

Annotons

Bacterial FadB hydroxyacyl-CoA dehydrogenase activity
fadb_hydroxyacyl_coa_dehydrogenase_activity
Participant: Family: bacterial FadB family
Family:
bacterial FadB familyInterPro:IPR012799
Representative Members: FadB (Pseudomonas putida KT2440)UniProtKB:Q88L02

Function

(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activityGO:0003857
Substrates: (3S)-3-hydroxyacyl-CoA NAD+
Products: 3-oxoacyl-CoA NADH proton

Processes

fatty acid beta-oxidationGO:0006635

The FadB dehydrogenase domain forms the 3-oxoacyl-CoA consumed by the FadA thiolase reaction.

Part 4: thiolytic two-carbon shortening
3-oxoacyl-CoA to acetyl-CoA and shortened acyl-CoAReactionbacterial_ketoacyl_coa_thiolysis

Annotons

Bacterial FadA 3-ketoacyl-CoA thiolase activity
fada_ketoacyl_coa_thiolase_activity
Participant: Family: bacterial FadA thiolase family
Family:
bacterial FadA thiolase familyInterPro:IPR012805
Representative Members: FadA (Pseudomonas putida KT2440)UniProtKB:Q88L01

Function

acetyl-CoA C-acyltransferase activityGO:0003988
Substrates: 3-oxoacyl-CoA coenzyme A
Products: acetyl-CoA fatty acyl-CoA shortened by two carbon atoms

Processes

fatty acid beta-oxidationGO:0006635

FadA releases acetyl-CoA and the shortened acyl-CoA that returns to the first reaction of the spiral.