PP_3198

UniProt ID: Q88I04
Organism: Pseudomonas putida KT2440
Review Status: COMPLETE
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Gene Description

PP_3198 encodes a compact Rieske [2Fe-2S]-binding ferredoxin-domain protein in the KT2440 flavonoid-degradation locus. KEGG assigns it to FdeD orthology group K26179 and the predicted naringenin hydroxylation step R13074. Its cofactor-binding role is well supported, but its electron donor, electron acceptor, and requirement for the proposed reaction remain untested.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0051537 2 iron, 2 sulfur cluster binding
IEA
GO_REF:0000002
ACCEPT
Summary: The Rieske domain and conserved ligand-rich region support [2Fe-2S] cluster binding.
Reason: UniProt, InterPro, Pfam, and sequence conservation independently identify a Rieske [2Fe-2S] domain.
Supporting Evidence:
file:PSEPK/PP_3198/PP_3198-uniprot.txt
InterPro; IPR017941; Rieske_2Fe-2S.
file:PSEPK/PP_3198/PP_3198-bioinformatics/RESULTS.md
Both proteins are compact Rieske [2Fe-2S]-domain proteins.
GO:0046275 flavonoid catabolic process
ISS
file:PSEPK/PP_3198/PP_3198-bioinformatics/RESULTS.md
REMOVE
Summary: Withdraw the inherited pathway-participation proposal; no FdeD-catalyzed or cofactor-dependent step has been established.
Reason: The locus, K26179 assignment and Rieske architecture identify a candidate, but neither PP_3198 nor Hsero_1006 has an established physiological electron donor, acceptor or flavonoid-catabolic step. Purified FdeE works without added FdeD; that does not exclude another role, but it supplies no positive evidence of participation by FdeD. The same-role comparators Hsero_1006 and bll6426 likewise decline a process assertion. Retain this inherited row for provenance while withdrawing the proposal; cluster binding remains supported and native pathway involvement remains a knowledge gap. No assertion of biological absence is made. The retired flag records deliberate withdrawal of this curator-authored proposal from the active set; it does not report disappearance of an upstream GOA annotation. REMOVE records withdrawal of this earlier curator-authored NEW proposal, not removal of a current GOA assertion. It does not claim that the protein is biologically incapable of participating in flavonoid catabolism.
Supporting Evidence:
file:PSEPK/PP_3198/PP_3198-bioinformatics/RESULTS.md
KEGG target mapping: `ppu:PP_3198 -> ko:K26179`
file:PSEPK/PP_3198/PP_3198-bioinformatics/RESULTS.md
Pairwise identity over aligned residue pairs: 45.6%

Core Functions

Rieske [2Fe-2S] cluster binding; physiological electron-transfer partners and catabolic role unresolved.

Supporting Evidence:
  • file:PSEPK/PP_3198/PP_3198-uniprot.txt
    InterPro; IPR017941; Rieske_2Fe-2S.
  • file:PSEPK/PP_3198/PP_3198-bioinformatics/RESULTS.md
    Both proteins are compact Rieske [2Fe-2S]-domain proteins.

References

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Suggested Questions for Experts

Q: Does PP_3198 transfer electrons to PP_3199 during naringenin hydroxylation in KT2440?

Suggested Experiments

Experiment: Reconstitute PP_3198, PP_3199, candidate cellular reductases, FAD, and naringenin; monitor electron transfer and hydroxylated product formation.

Type: biochemical reconstitution

Knowledge Gaps

What is not known β€” curated, literature-grounded statements of the open unknowns (the inverse of core functions).

Gap: The electron donor and physiological electron acceptor of PP_3198 are unknown.

OPEN BIOLOGYCURATION

What is known: K26179 placement associates PP_3198 with R13074, but available evidence does not establish direct electron transfer to PP_3199/FdeE or another enzyme.

Significance: Partner identity is needed before assigning a specific oxidoreductase activity or complex.

What would resolve it: Reconstitute PP_3198 with candidate reductases and FdeE-family proteins while monitoring electron transfer and product formation.

Provenance (the field's own admissions):

πŸ“š Additional Documentation

Notes

(PP_3198-notes.md)

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Bioinformatics Results

(RESULTS.md)

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