Gene Ontology annotation based on Enzyme Commission mapping
TreeGrafter-generated GO annotations
UniProtKB entry Q88RQ2 for Pseudomonas putida KT2440 BetC
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Q88RQ2 is assigned EC 3.1.6.6.
"EC=3.1.6.6"
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The target contains the specific InterPro choline-sulfatase signature.
"InterPro; IPR017785; Choline-sulfatase."
Uncoupling of choline-O-sulphate utilization from osmoprotection in Pseudomonas putida.
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KT2440 betC is required to use choline-O-sulfate as a carbon or nitrogen source but not to accumulate it.
"This mutant still accumulated intact COS but failed to use this compound as carbon or nitrogen source."
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High salt downregulates betC, supporting metabolism rather than osmoprotection as its main KT2440 role.
"the principal role of this gene lied in COS metabolism, not in osmoprotection"
Presence of a gene encoding choline sulfatase in Sinorhizobium meliloti bet operon: choline-O-sulfate is metabolized into glycine betaine.
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Sinorhizobium BetC directly converts choline-O-sulfate and, more slowly, phosphorylcholine to choline.
"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."
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Loss of betC eliminates choline-sulfatase activity in the ortholog system.
"Choline sulfatase activity was absent from betC but not from betB mutants"
Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester.
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Purified Sinorhizobium choline sulfatase efficiently hydrolyzes choline-O-sulfate.
"Sinorhizobium meliloti choline sulfatase (SmCS) efficiently catalyzes the hydrolysis of alkyl sulfate choline-O-sulfate"
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The crystal structure defines the active site of this BetC exemplar.
"Its 2.8-Å resolution X-ray structure shows a buried, largely hydrophobic active site"
OpenScientist deep-research report for PSEPK betC
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The report identifies the exact target and conserved choline-sulfatase motif.
"A direct sequence scan locates the universal sulfatase active-site signature **(C/S)-X-P-X-R** as **C52-A-P-S-R56** near the N-terminus."
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The report explicitly notes the absence of purified KT2440 Q88RQ2 enzymology.
"No direct enzymology on the *P. putida* protein itself."