moeA encodes a soluble molybdopterin molybdenumtransferase that inserts molybdate into adenylylated molybdopterin, releases AMP, and forms Mo-molybdopterin. This reaction completes the conserved metal-insertion stage of molybdenum-cofactor biosynthesis before optional nucleotide maturation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005737 cytoplasm | IEA GO_REF:0000118 | MARK AS OVER ANNOTATED | Summary: Cytoplasm is a redundant parent of the more specific retained cytosol annotation. Reason: Q88L14 acts in the soluble cytosol; retaining both cytoplasm and cytosol adds no distinct localization information. |
| GO:0005829 cytosol | IEA GO_REF:0000118 | KEEP AS NON CORE | Summary: Cytosol is an appropriate specific localization for MoeA. Reason: The molybdate-insertion reaction occurs in the soluble cofactor biosynthetic pathway. |
| GO:0006777 Mo-molybdopterin cofactor biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: MoeA directly forms Mo-molybdopterin during cofactor biosynthesis. Reason: UniProt assigns the adenylyl-MPT plus molybdate reaction producing Mo-MPT. |
| GO:0032324 molybdopterin cofactor biosynthetic process | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: This broad process is redundant with the more specific retained Mo-molybdopterin cofactor biosynthetic process annotation. Reason: MoeA directly produces Mo-MPT, so GO:0006777 captures its pathway role more precisely than this parent term. |
| GO:0046872 metal ion binding | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: Metal-ion binding is compatible with molybdate insertion and Mg2+-dependent catalysis but is non-core. Reason: UniProt records Mg2+ and molybdate in the MoeA reaction; the exact catalytic term is more informative. |
| GO:0061599 molybdopterin molybdotransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This is the exact core molecular function of MoeA. Reason: UniProt supplies EC 2.10.1.1 and the reaction converting adenylyl-MPT plus molybdate to Mo-MPT plus AMP. Supporting Evidence: file:PSEPK/moeA/moeA-uniprot.txt CC -!- CATALYTIC ACTIVITY: CC Reaction=adenylyl-molybdopterin + molybdate = Mo-molybdopterin + AMP + CC H(+); Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, CC ChEBI:CHEBI:62727, ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; CC EC=2.10.1.1; Evidence={ECO:0000256|ARBA:ARBA00047317}; file:PSEPK/moeA/moeA-deep-research-openscientist.md > **adenylyl-molybdopterin (MPT-AMP) + molybdate (MoO₄²⁻) → Mo-molybdopterin (Moco) + AMP + H⁺** (Mg²⁺-dependent) |
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Download this section (compressed HTML)Q: Which KT2440 protein supplies the preceding MPT adenylyltransferase activity required by MoeA?
Experiment: Reconstitute Mo-MPT formation with Q88L14 and candidate MPT-adenylylating proteins, measuring adenylyl-MPT, AMP release, and Mo-MPT formation.
Type: biochemical pathway reconstitution
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