Gene Ontology annotation through association of InterPro records with GO terms
Electronic Gene Ontology annotations created by ARBA machine learning models
UniProtKB entry Q88I07 for Pseudomonas putida KT2440 PP_3195
Genetic and functional characterization of a novel meta-pathway for degradation of naringenin in Herbaspirillum seropedicae SmR1.
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The Herbaspirillum fde pathway performs naringenin A-ring cleavage, but FdeB itself was not among the directly tested enzymes.
"naringenin is first mono-oxygenated by the FdeE protein"
OpenScientist deep research report on PP_3195 (Q88I07)
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The report identifies the K26184/R13077 prediction and explicitly notes that PP_3195 has no direct biochemical or genetic characterization.
"No direct biochemical or genetic characterization of PP_3195/FdeB itself has been published."
Reproducible PP_3195 and Hsero_1004 sequence comparison
OpenScientist hypothesis report for PP_3195 serine-type peptidase activity
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OpenScientist judged the serine-type peptidase annotation over-annotated and favoured an ester or lactone hydrolase identity (FdeB).
"far too small** to contain the ~250–300-aa seven-bladed β-propeller that is a defining, substrate-gating feature of bona fide S9-family peptidases"
Flavonoid follow-up source checks and FdeB inference boundaries
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The FrsA-like family includes a characterized C-C hydrolase, so membership does not resolve ester specificity.
"Plays a role in nicotine catabolism by cleaving a C-C bond in 2,6-dihydroxypseudooxynicotine"
An alpha/beta-fold C--C bond hydrolase is involved in a central step of nicotine catabolism by Arthrobacter nicotinovorans.
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The characterized Q93NG6 family comparator hydrolytically cleaves a nicotine-derived C-C substrate; FrsA-like family membership does not imply ester specificity.
"The enzyme catalyzing the hydrolytic cleavage of 2,6-dihydroxypseudooxynicotine to 2,6-dihydroxypyridine and gamma-N-methylaminobutyrate"
Structure and action of a C-C bond cleaving alpha/beta-hydrolase involved in nicotine degradation.
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The characterized Arthrobacter C-C hydrolase has a 2.1-A alpha/beta-hydrolase structure and a substrate model supported by activity measurements of 11 point mutants. The substrate was modeled rather than crystallographically bound; this is comparator evidence, not an FdeB target assay.
"The model was supported by enzymatic activity data of 11 point mutants"
Reproducible mapping of four Q93NG6 active-site positions to the FdeB panel
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The E148 counterpart is aspartate, retaining acidic character but not residue identity; all four positions remain sequence-based candidate assignments without target mutagenesis or geometry.
"PP_3195: query E148/S217/D300/H329 maps to D195/S268/D359/H394."
FdeB candidate-site comparison and provider-numbering adjudication
Official reviewed UniProtKB Q93NG6 record snapshot
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Q93NG6 is an experimentally characterized C-C hydrolase and an IPR050261 family comparator; this does not transfer nicotine-substrate specificity to FdeB.
"Plays a role in nicotine catabolism by cleaving a C-C bond in 2,6-dihydroxypseudooxynicotine"
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The Q93NG6 E148A mutagenesis feature reports 98% activity loss with ECO:0000269 attributed to PMID:17275835. Its separate E148 active-site feature uses ECO:0000255/ECO:0000303. S217A is also experimentally annotated with total activity loss; E148 is important but not uniquely the strongest perturbation.
"98% loss of activity."