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The report states the conserved MoeB acyl-adenylation reaction, independently supported by target UniProt.
"**The reaction catalyzed is: MoaD-COO⁻ + ATP → MoaD-CO-AMP (MoaD-adenylate) + PPᵢ.**"
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The report explicitly acknowledges that no direct Q88PW3 assay, structure, or knockout was found.
"**No direct experimental characterization of Q88PW3 itself.** The functional assignment is inferred from the *E. coli* ortholog (P12282) via high sequence identity (~54%) and conserved motifs. No published enzymatic assay, structure, or knockout of the *P. putida* PP_0735 protein was identified."
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The report presents a target-specific alignment that was not saved as a reproducible local artifact.
"A Needleman-Wunsch global alignment of the two proteins (251 aa vs. 249 aa) yields **133 identical residues = 53.8% identity** over aligned columns (53.0% over the full Q88PW3 length), with near-identical length and no large insertions or deletions (alignment length 253)."
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The report presents target motif and zinc-site calls that were not saved as a reproducible local artifact.
"Two cysteine-pair motifs — `CYHC` (C171–C174) and `CTVC` (C243–C246, at the extreme C-terminus) — match the structural zinc-binding site characteristic of *E. coli* MoeB."
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Q88PW3 is a classical 251-aa MoeB without a fused rhodanese domain, separating adenylation from sulfur transfer.
"Q88PW3 is therefore a "classic" adenylyltransferase that requires a separate downstream sulfurtransferase to complete thiocarboxylation."
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The report explicitly identifies lack of a direct target-specific assay while supporting functional transfer from E. coli.
"No direct experimental characterization of Q88PW3 itself."