moaB-II encodes a soluble MoaB-family protein located near canonical moaA. MoaB-family proteins bind GTP and molybdopterin, but catalytic MPT adenylyltransferase activity is lineage-dependent; the exact biochemical contribution and necessity of this KT2440 paralog remain unresolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005829 cytosol | IEA GO_REF:0000118 | KEEP AS NON CORE | Summary: Cytosolic localization is compatible with this small soluble MoaB-family protein. Reason: Q88E67 lacks membrane/export features and occurs in a soluble cofactor-biosynthesis neighborhood. |
| GO:0006777 Mo-molybdopterin cofactor biosynthetic process | IEA GO_REF:0000120 | UNDECIDED | Summary: Pathway involvement is plausible but the paralog's exact contribution and necessity are unresolved. Reason: UniProt says MoaB may participate but explicitly transfers a no-MPT-adenylyltransferase statement from the family; no gene-specific assay establishes Q88E67's role. Supporting Evidence: file:PSEPK/moaB-II/moaB-II-uniprot.txt CC -!- FUNCTION: May be involved in the biosynthesis of molybdopterin. Can CC bind GTP and has low GTPase activity. Can bind MPT, but has no MPT CC adenylyl transferase activity. {ECO:0000256|ARBA:ARBA00055616}. file:PSEPK/moaB-II/moaB-II-deep-research-openscientist.md The caveat is not mis-identification but *evidence type*: there is **no primary experimental study of the P. putida protein Q88E67 itself**; its annotation is by homology to characterized family members. |
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Download this section (compressed HTML)Q: Does Q88E67 catalyze MPT adenylylation, act as a noncatalytic pathway partner, or have no required role in KT2440 Mo-cofactor biosynthesis?
Experiment: Compare purified Q88E67 with Q88L15 in MPT-binding, ATP-dependent MPT adenylylation, and MoeA-coupled Mo-MPT formation assays.
Type: comparative biochemical assay
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