SerB is phosphoserine phosphatase, the terminal enzyme of the phosphorylated L-serine biosynthetic pathway. It hydrolyzes O-phospho-L-serine to L-serine and phosphate.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000287 magnesium ion binding | IEA GO_REF:0000118 | KEEP AS NON CORE | Summary: Retain as a non-core cofactor-binding property distinct from the substrate-specific catalytic activity. Reason: The Q88DB8 record assigns Mg2+ and places the protein in the Mg2+-dependent HAD-like SerB family. Supporting Evidence: file:PSEPK/serB/serB-uniprot.txt Name=Mg(2+) PMID:11342136 PSP and P-type ATPases utilize a common mechanism that involves Mg(2+)-dependent phosphorylation and autodephosphorylation at an aspartyl side chain in the active site. |
| GO:0005737 cytoplasm | IEA GO_REF:0000118 | KEEP AS NON CORE | Summary: Cytoplasmic localization is plausible but is not a defining catalytic property. Reason: TreeGrafter provides indirect phylogenetic support for cytoplasmic localization, but no direct localization experiment is available for Q88DB8. Retain the annotation as secondary context rather than core function. Supporting Evidence: GO_REF:0000118 |
| GO:0006564 L-serine biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: Accept by conserved reaction-role inference from characterized bacterial phosphoserine phosphatases. Reason: Characterized SerB enzymes convert O-phospho-L-serine to L-serine, the terminal reaction of the phosphorylated biosynthetic pathway. Supporting Evidence: PMID:25037224 Phosphoserine phosphatase (PSP), a key essential metabolic enzyme involved in conversion of O-phospho-l-serine to l-serine, was characterized in this study. |
| GO:0036424 L-phosphoserine phosphatase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Accept the enzyme-specific function by conserved-family inference from biochemically characterized bacterial SerB enzymes. Reason: Q88DB8 has the HAD-like SerB family architecture, Mg2+ cofactor assignment, and the same substrate-specific role characterized in bacterial orthologs. Supporting Evidence: file:PSEPK/serB/serB-uniprot.txt TIGR00338; serB PMID:25037224 Phosphoserine phosphatase (PSP), a key essential metabolic enzyme involved in conversion of O-phospho-l-serine to l-serine, was characterized in this study. |
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Download this section (compressed HTML)Experiment: Test a clean serB deletion for serine auxotrophy and restore growth by L-serine supplementation or gene complementation.
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