Fermentation

METPO:1002005 · CLASS · REVIEWED

A respiration that generates energy through the oxidation of organic compounds without using an external electron acceptor, using organic molecules as both electron donors and final electron acceptors.

Fermentation redox and substrate-level phosphorylation

Evidence-backed causal sketch linking organic substrate redox balancing to fermentative ATP generation.

Fermentation redox and substrate-level phosphorylation Interactive directed graph showing evidence-backed causal relationships for Fermentation.

Edge evidence

  • Fermentation uses organic substrate

    Fermentation uses an organic substrate as both electron donor and acceptor source.

    • DOI:10.3389/fmicb.2021.703525 substrate of a fermentation has to serve as electron donor as well as acceptor Supports organic substrate donor/acceptor role.
  • organic substrate oxidation reduces reduced redox cofactors

    Substrate oxidation generates reduced redox cofactors.

    • DOI:10.1111/1751-7915.13746 a substrate is oxidized to an intermediate Review describes substrate oxidation with cofactor reduction in fermentation.
  • reduced redox cofactors reoxidized by fermentation products

    Product-forming reductions regenerate oxidized cofactors.

    • DOI:10.1111/1751-7915.13746 after which the intermediate is reduced Supports product-side reduction and redox cofactor regeneration.
  • Fermentation conserves energy by substrate-level phosphorylation

    Substrate-level phosphorylation is a major fermentative energy-conservation route.

    • DOI:10.1111/1751-7915.13746 main sources of energy under fermentative conditions Supports SLP as a fermentative energy mechanism.
  • substrate-level phosphorylation produces ATP METPO:2000202

    Substrate-level phosphorylation directly forms ATP.

    • DOI:10.1111/1751-7915.13746 energy-rich bonds (for example via substrate-level phosphorylation) Supports SLP as ATP-linked energy conservation.
  • Fermentation excludes external inorganic terminal electron acceptor

    Fermentation excludes use of external inorganic terminal electron acceptors, distinguishing it from anaerobic respiration.

    • DOI:10.1093/femsre/fuae016 Excludes processes that use external inorganic terminal acceptors, explicitly naming nitrate and sulfur respiration.
  • glycolysis (Embden-Meyerhof-Parnas pathway) feeds into pyruvate

    Glycolysis (EMP) feeds carbon flux to pyruvate, the entry point for fermentation branches.

    • DOI:10.1093/femsre/fuae016 Glycolysis (EMP) and the pentose phosphate pathway feed to pyruvate.
  • pyruvate:ferredoxin oxidoreductase produces reduced ferredoxin METPO:2000202

    Pyruvate:ferredoxin oxidoreductase oxidizes pyruvate and produces reduced ferredoxin.

    • DOI:10.1093/femsre/fuae016 Pyruvate:ferredoxin oxidoreductase produces reduced ferredoxin; central to redox balancing.
  • ferredoxin:NAD+ oxidoreductase transfers electrons from reduced ferredoxin to NAD+

    Ferredoxin:NAD+ oxidoreductase reoxidizes reduced ferredoxin by transferring electrons to NAD+.

    • DOI:10.1093/femsre/fuae016 Ferredoxin-NAD+ reductase transfers electrons from reduced ferredoxin to NAD+; strong redox-balancing edge.
  • flavin-based electron bifurcation reduces reduced ferredoxin METPO:2000017

    Flavin-based electron bifurcation couples exergonic and endergonic redox reactions, reducing low-potential ferredoxin.

    • DOI:10.1038/s41467-023-41212-x Couples an exergonic and an endergonic redox reaction within a single soluble enzyme complex, typically reducing low-potential ferredoxin.
  • ion-motive force drives ATP synthase

    Ion-motive force generated during fermentation drives ATP synthase-mediated ATP formation.

    • DOI:10.1093/femsre/fuae016 Ion gradients drive ATP synthesis via ATP synthases; links fermentation to chemiosmotic ATP conservation.
  • ATP synthase produces ATP METPO:2000202

    ATP synthase forms ATP using the ion-motive force.

    • DOI:10.1093/femsre/fuae016 ATP synthesis via ATP synthases driven by ion gradients during fermentation.

Provenance

Source
METPO (2025-11-25)
Author
Luke Wang
Definition source
DOI:10.3389/fmicb.2021.703525

Parent traits (1)

kg-microbe context

Matched 1 kg-microbe node via direct_metpo.

  • METPO:1002005 [-0.758, -6.428, +3.551, +10.454, …]

512-dim DeepWalkSkipGramEnsmallen embedding from kg-microbe (2026-04-25).

Nearest neighbors in embedding space

Top-8 cosine-similar METPO traits from the 2026-04-25 deepwalk (512-D).

Curation history

  1. · SEEDED_FROM_METPO · seed_from_metpo

    imported from data/raw/metpo.owl (CLASS)

  2. · ADDED_CAUSAL_GRAPH · codex

    Added DOI-backed causal graph for fermentation redox balancing and substrate-level phosphorylation.

  3. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 1 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (METPO:2000202×1).

  4. · REMOVE_REDUNDANT_SYNONYM · claude

    Removed 1 synonym(s) whose text duplicated the label (seeder redundancy; no information lost).

  5. · ENRICH_CAUSAL_GRAPH · claude

    Added 7 evidence-backed generic edges (10 new nodes) from the deep-research report.

  6. · GROUND_CAUSAL_PREDICATES · claude

    Grounded 3 causal-edge predicate_id field(s) via mappings/predicate_grounding.tsv (METPO:2000202×2, METPO:2000017×1).

  7. · GROUND_CAUSAL_NODES · claude

    Grounded 1 causal-node grounding field(s) via mappings/node_grounding.tsv (UniProtKB:A0A415TT77×1).

  8. · GROUND_CAUSAL_NODES · claude

    Grounded 3 causal-node grounding field(s) via mappings/node_grounding.tsv (CHEBI:15361×1, CHEBI:17513×1, CHEBI:15846×1).

  9. · GROUND_CAUSAL_NODES · claude

    Grounded 2 causal-node grounding field(s) via mappings/node_grounding.tsv (UniProtKB:A0A075WCC3×1, UniProtKB:I3R731×1).