BetC is a cytoplasmic choline sulfatase that hydrolyzes choline-O-sulfate to choline, sulfate, and a proton. In Pseudomonas putida KT2440 it supports use of choline-O-sulfate as a carbon or nitrogen source; unlike BetA/BetB-mediated glycine-betaine production, its principal role is choline-O-sulfate metabolism rather than osmoprotection.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005737 cytoplasm | IEA GO_REF:0000118 | KEEP AS NON CORE | Summary: Retain the phylogenetically inferred cytoplasmic localization as non-core. Reason: The TreeGrafter annotation is not contradicted by the target sequence or pathway context, but location is ancillary to the catalytic function. Supporting Evidence: file:PSEPK/betC/betC-goa.tsv GO:0005737 cytoplasm file:PSEPK/betC/betC-deep-research-openscientist.md Localization inferred from phenotype, not from imaging. |
| GO:0008484 sulfuric ester hydrolase activity | IEA GO_REF:0000118 | KEEP AS NON CORE | Summary: Retain this chemically valid broad parent as non-core. Reason: BetC hydrolyzes a sulfate ester, but the existing exact choline-sulfatase term is more informative for its core function. Supporting Evidence: file:PSEPK/betC/betC-goa.tsv GO:0008484 sulfuric ester hydrolase activity |
| GO:0047753 choline-sulfatase activity | IEA GO_REF:0000003 | ACCEPT | Summary: Accept exact choline-sulfatase activity as the core molecular function. Reason: The target has concordant EC 3.1.6.6 and choline-sulfatase-specific domain assignments, KT2440 betC genetics support choline-O-sulfate utilization, and the reviewed Sinorhizobium BetC exemplar has direct genetic and enzymatic evidence for the same reaction. Supporting Evidence: file:PSEPK/betC/betC-uniprot.txt InterPro; IPR017785; Choline-sulfatase. PMID:17116241 This mutant still accumulated intact COS but failed to use this compound as carbon or nitrogen source. PMID:9736747 a new gene (betC) was identified as encoding a choline sulfatase catalyzing the conversion of choline-O-sulfate and, at a lower rate, phosphorylcholine, into choline. PMID:29458126 Sinorhizobium meliloti choline sulfatase (SmCS) efficiently catalyzes the hydrolysis of alkyl sulfate choline-O-sulfate file:PSEPK/betC/betC-deep-research-openscientist.md No direct enzymology on the *P. putida* protein itself. |
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Download this section (compressed HTML)Q: What are the kinetic parameters and in vivo contributions of KT2440 BetC for choline-O-sulfate versus phosphorylcholine?
Experiment: Purify Q88RQ2 and quantify choline-O-sulfate and phosphorylcholine hydrolysis, then compare metabolite flux and growth in clean betC deletion and complementation strains under carbon-, nitrogen-, and sulfur-source conditions.
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