Benzoate upper degradation pathway

A reusable bacterial aromatic-catabolism module for the upper benzoate degradation route that converts benzoate to catechol. The pathway begins with a multicomponent benzoate 1,2-dioxygenase system, represented here by BenA-like large oxygenase, BenB-like small oxygenase, and BenC-like reductase roles, and is followed by a BenD-like cis-diol dehydrogenase. Pseudomonas putida KT2440 benA/benB/benC/benD provide the local PSEPK exemplars for this module, but the module boundary is the conserved benzoate-to-catechol pathway segment rather than a PSEPK-specific locus definition.

MODULE:benzoate_upper_pathwayDRAFTCONCRETEMetabolic Pathwaymodules/benzoate_upper_pathway.yaml
benzoate catabolic process via hydroxylationGO:0043639
GO:0043639
benzoate catabolic process
GO:0043639 grounds the module. The route-specific term GO:0043640 (benzoate catabolic process via hydroxylation) was obsoleted in GO release 2026-07-26 with replaced_by GO:0043639; the hydroxylation route, dioxygenation of benzoate to a cis-dihydrodiol intermediate followed by dehydrogenation to catechol, is carried by the module structure.
KEGG:ppu00622
Pseudomonas putida KT2440 xylene degradation
The PSEPK partition table assigns benA, benB, benC, and benD as the primary KT2440 genes in KEGG ppu00622 for this upper benzoate route.
KEGG:M00551
Benzoate degradation, benzoate to catechol
KEGG module M00551 captures the narrower benzoate-to-catechol pathway boundary implemented by benA, benB, benC, and benD; this is the preferred biochemical anchor for the module over the broader ppu00622 map label.
file:projects/P_PUTIDA/data/psepk_pathway_membership.tsv
PSEPK pathway membership table
The local membership table lists benA, benB, benC, and benD in ppu00622 and overlapping aromatic-catabolism maps, while PP_1791 and PP_2504 are ppu00621 lower-pathway spillover genes and are outside this module.
PMID:12534466
Genomic analysis of the aromatic catabolic pathways from Pseudomonas putida KT2440
The KT2440 aromatic-catabolism map places the ben genes in a benzoate peripheral pathway feeding catechol into the beta-ketoadipate route.
PMID:11053377
BenR, a XylS homologue, regulates three different pathways of aromatic acid degradation in Pseudomonas putida.
The BenR study identifies benABC as likely encoding the benzoate dioxygenase system and supports co-regulated benzoate-responsive expression.
file:PSEPK/benA/benA-ai-review.yaml
Curated benA review
The benA review accepts benzoate 1,2-dioxygenase activity and benzoate catabolism via hydroxylation as core functions of the large oxygenase subunit.
file:PSEPK/benB/benB-ai-review.yaml
Curated benB review
The benB review treats BenB as a beta subunit contributing to the BenABC dioxygenase complex and removes a propagated 3-phenylpropionate process assignment.
file:PSEPK/benC/benC-ai-review.yaml
Curated benC review
The benC review accepts ferredoxin-NAD+ reductase activity and contribution to benzoate 1,2-dioxygenase activity as the electron-transfer role for the pathway's first step.
file:PSEPK/benD/benD-ai-review.yaml
Curated benD review
The benD review accepts the exact cis-diol dehydrogenase activity and removes a propagated fatty-acid elongation process assignment.
file:modules/benzoate_upper_pathway-deep-research-openscientist.md
OpenScientist module research for benzoate upper degradation
OpenScientist module-level research supports the benzoate-to-catechol boundary, the obligatory ordering of BenABC dioxygenation before BenD dehydrogenation, and the exclusion of downstream catechol cleavage and CoA-dependent benzoate routes from this module.
file:projects/P_PUTIDA/deep-research/PSEPK__benzoate_upper_pathway__ppu00622-deep-research-openscientist.md
OpenScientist PSEPK ppu00622 benzoate upper-pathway review
OpenScientist concluded that the benzoate upper pathway is covered by benA/benB/benC/benD, that PP_1791 and PP_2504 are lower meta-cleavage spillover candidates, and that the ppu00622 xylene map label is broader than the endogenous KT2440 benzoate-to-catechol route.
PMID:42567519
Structural basis for oxidative decarboxylation of lignin-derived aromatics by the fungal flavoprotein monooxygenase PcMNX1.
Assessed as a candidate member and declined. PcMNX1 performs decarboxylative hydroxylation of lignin-derived aromatic acids to hydroquinones, which is neither of this module's two reactions and does not yield the cis-dihydrodiol that BenD consumes; the paper is cited here only to record the boundary it helps delimit.
Recombinant PcMNX1 catalyzed the NAD(P)H-dependent oxidative decarboxylation of SA to dimethoxyhydroquinone (DMHQ) and also converted other lignin-derived aromatics, including vanillic acid and 4-hydroxybenzoic acid

First-pass PSEPK interpretation: benA/benB/benC/benD satisfy the upper benzoate degradation segment from benzoate to catechol. The broader KEGG ppu00622 "xylene degradation" bucket intersects several aromatic maps, but this module deliberately stops at catechol; catechol ring cleavage, 2-hydroxymuconate/4-oxalocrotonate steps, and the PP_1791/PP_2504 ppu00621 spillover genes belong in downstream catechol/meta-cleavage modules. The module also keeps the electron-transfer and oxygenase roles separate so that BenC is not represented as independently enabling the terminal oxygenase chemistry. CANDIDATE ASSESSED, NOT MODELLED — PcMNX1 (PMID:42567519): a 2026 report identifies PcMNX1, a group A flavoprotein monooxygenase from the white-rot fungus Phanerodontia (Phanerochaete) chrysosporium, as the enzyme performing NAD(P)H-dependent oxidative decarboxylation of the syringyl-unit intermediate syringate to dimethoxyhydroquinone, and also reports conversion of vanillate and 4-hydroxybenzoate — the cached abstract does not state the products for those two substrates. It is deliberately not added as a member here, for three reasons. (i) Chemistry: this module contains exactly two reactions — Rieske-type multicomponent dioxygenation of benzoate to cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate (GO:0018623), then NAD+-dependent cis-diol dehydrogenation to catechol (GO:0047116). PcMNX1 is a single-component group A FAD monooxygenase whose product is a hydroquinone, not the multicomponent Rieske dioxygenase plus SDR dehydrogenase pair modelled here, so it neither occupies an existing step nor supplies the cis-dihydrodiol BenD requires; accommodating it would redefine what this module is rather than extend its membership. (CO2 release is not itself a discriminator: BenD's own dehydrogenation step is decarboxylating and lists carbon dioxide among its products.) (ii) Substrate, route, and taxon: the physiological substrate is syringate, the products belong to the fungal lignin-aromatic hydroquinone route rather than the benzoate-to-catechol-to-beta-ketoadipate route this module feeds, benzoate itself is not among the reported substrates, and the module's declared context taxon is NCBITaxon:2 Bacteria. The reported vanillate activity is likewise a different fate for vanillate than the VanAB O-demethylation to protocatechuate modelled in hydroxycinnamate_vanillate_catabolism.yaml, so that module is not an alternative home either. (iii) Grounding: participants here are FAMILY selectors carrying an InterPro family id plus UniProtKB representative members, and no UniProtKB accession for PcMNX1 itself was retrievable — UniProt returns no entry cross-referencing PMID:42567519, and no entry for Phanerochaete chrysosporium under the gene name MNX1. The related GsMNX1 of Gelatoporia (Ceriporiopsis) subvermispora, which the same abstract names, was likewise not retrievable under that gene name, but it was not run down further; the gene symbol MNX1 is not unused in fungi (UniProtKB:G8B709, a Candida parapsilosis FAD-binding protein, carries it), so the searched-and-not-found claim here is deliberately narrow. The paper itself is cached abstract-only. Re-evaluate if a fungal lignin-derived aromatic catabolism module is created; that paper, with the GsMNX1 comparison and the bacterial 3-hydroxybenzoate 6-hydroxylase active-site analysis it reports, is good source material for one. This candidate is also recorded as a structured, queryable entry in this module's knowledge_gaps block (status OPEN), which carries the reference-level judgment and the re-evaluation trigger in machine-readable form.

3Nodes
2Parts
0Variant Sets
0Variants
4Annotons
1Connections

Derived QC

Recommended-field compliance

90.0% recommended fields populated
  • references[0] · findings (0/1)

Module deep research

✓ present

  • benzoate_upper_pathway-deep-research-openscientist.md (openscientist)

Leaf nodes lacking representative members

✓ every leaf node grounds to a representative protein.

Template conformance

✓ every declared conforms_to bundle matches its template motif.

Reaction chaining (advisory)

✓ every PRECEDES step chains, or its break is acknowledged via chaining_status.

  • benabc_dioxygenation → bend_dehydrogenation [NOT_CHECKED]

Gene-review completeness (4/4 grounded genes reviewed)

4 complete review(s) · 4 with deep research · 0 missing review · 0 reviewed but lacking deep research

Gene Review Complete Deep research
benA Q88I40 ✓ ✓ ✓
benB Q88I39 ✓ ✓ ✓
benC Q88I38 ✓ ✓ ✓
benD Q88I37 ✓ ✓ ✓

Details

Context
bacteriaNCBITaxon:2
cytosolGO:0005829
Benzoate to catechol upper pathwayMetabolic Pathwaybenzoate_upper_pathway
benzoate catabolic process via hydroxylationGO:0043639
Context
bacteriaNCBITaxon:2
cytosolGO:0005829

Connections

The cis-dihydrodiol produced by BenABC is the substrate for BenD.
Part 1: benzoate dioxygenation to a cis-dihydrodiol
BenABC benzoate dioxygenationReactionbenabc_dioxygenation

A multicomponent benzoate 1,2-dioxygenase system introduces both atoms of dioxygen into benzoate, producing the cis-dihydrodiol intermediate used by the downstream dehydrogenase step.

Annotons

Benzoate 1,2-dioxygenase large oxygenase subunit
bena_large_oxygenase
Participant: Family: benzoate 1,2-dioxygenase large subunit family
Family:
benzoate 1,2-dioxygenase large subunit familyInterPro:IPR017639 BenA-like ring-hydroxylating dioxygenase alpha/large subunits containing the Rieske and catalytic oxygenase domains.
Representative Members: PSEPK benA exemplarUniProtKB:Q88I40

Function

benzoate 1,2-dioxygenase activityGO:0018623
Substrates: benzoate dioxygen NADH
Products: cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate NAD+
Cofactors: Rieske [2Fe-2S] clusterGO:0051537 non-heme ironGO:0005506

Processes

benzoate catabolic process via hydroxylationGO:0043639

Locations

cytosolGO:0005829

Terminal oxygenase large subunit that carries the Rieske electron-transfer cluster and catalytic non-heme iron site for benzoate cis-dihydroxylation.

Benzoate 1,2-dioxygenase small oxygenase subunit
benb_small_oxygenase
Participant: Family: benzoate 1,2-dioxygenase small subunit family
Family:
benzoate 1,2-dioxygenase small subunit familyInterPro:IPR017641 BenB-like ring-hydroxylating dioxygenase beta/small subunits that support the terminal oxygenase component.
Representative Members: PSEPK benB exemplarUniProtKB:Q88I39

Function

contributes to benzoate 1,2-dioxygenase activityGO:0018623
Substrates: benzoate dioxygen
Products: cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate

Processes

benzoate catabolic process via hydroxylationGO:0043639

Locations

cytosolGO:0005829

Small oxygenase subunit that contributes to the BenAB terminal oxygenase component rather than independently catalyzing the full dioxygenase reaction.

Benzoate dioxygenase reductase/electron-transfer component
benc_electron_transfer
Participant: Family: BenC-like FAD/NAD-binding reductase family
Family:
BenC-like FAD/NAD-binding reductase familyInterPro:IPR047683 BenC-like reductase components that provide electrons to the terminal benzoate dioxygenase oxygenase.
Representative Members: PSEPK benC exemplarUniProtKB:Q88I38

Function

ferredoxin-NAD+ reductase activityGO:0008860
Substrates: NADH oxidized BenC [2Fe-2S] center
Products: NAD+ reduced BenC [2Fe-2S] center
Cofactors: FADGO:0050660 [2Fe-2S] clusterGO:0051537

Processes

benzoate catabolic process via hydroxylationGO:0043639

Locations

cytosolGO:0005829

Reductase/electron-transfer component that supplies reducing equivalents needed by the BenAB oxygenase through a fused FAD/[2Fe-2S] electron-transfer chain; this is modeled as its own redox function plus contribution to the dioxygenase step.

Part 2: cis-dihydrodiol dehydrogenation to catechol
BenD cis-diol dehydrogenationReactionbend_dehydrogenation

BenD-like dehydrogenases oxidize the benzoate cis-dihydrodiol intermediate generated by BenABC, yielding catechol for downstream beta-ketoadipate or catechol-cleavage modules.

Annotons

Benzoate cis-dihydrodiol dehydrogenase
bend_cis_diol_dehydrogenase
Participant: Family: BenD dehydrogenase family
Family:
BenD dehydrogenase familyInterPro:IPR047686 BenD-like SDR-family enzymes catalyzing oxidation of the benzoate cis-dihydrodiol intermediate.
Representative Members: PSEPK benD exemplarUniProtKB:Q88I37

Function

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase activityGO:0047116
Substrates: cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate NAD+
Products: catechol NADH carbon dioxide

Processes

benzoate catabolic process via hydroxylationGO:0043639

Locations

cytosolGO:0005829

Dehydrogenation step converting the BenABC product to catechol.