mobA encodes the cytoplasmic molybdenum-cofactor guanylyltransferase that transfers GMP from GTP to Mo-molybdopterin, producing the MGD cofactor variant used by a subset of molybdoenzymes. This is an optional nucleotide-maturation branch downstream of conserved Mo-MPT formation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MODIFY | Summary: Generic catalytic activity should be replaced by the exact MobA reaction. Reason: Reviewed UniProt/HAMAP assigns EC 2.7.7.77 Mo-MPT guanylyltransferase activity. Proposed replacements: molybdenum cofactor guanylyltransferase activity Supporting Evidence: file:PSEPK/mobA/mobA-uniprot.txt CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) CC cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine CC dinucleotide (Mo-MGD) cofactor. {ECO:0000255|HAMAP-Rule:MF_00316}. |
| GO:0005525 GTP binding | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: GTP binding is valid substrate binding but less informative than the catalytic term. Reason: GTP donates GMP in the MobA reaction, and the HAMAP GTP-binding residues are annotated on Q88HA3; the E. coli MobA-GTP cocrystal places GTP in the N-terminal half. Substrate binding is a component of the guanylyltransferase activity, so non-core, as in ECOLI/mobA. Supporting Evidence: file:PSEPK/mobA/mobA-uniprot.txt /ligand="GTP" PMID:10978347 The cocrystal structure of MobA and GTP reveals that the GTP-binding site is located in the N-terminal half of the molecule. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Cytoplasmic localization is appropriate for this soluble cofactor-maturation enzyme. Reason: Q88HA3 lacks membrane/export features and acts on soluble Mo-MPT. No cytosol-specific evidence exists for MobA, so cytoplasm is as precise as warranted; same action as ECOLI/mobA. Supporting Evidence: file:PSEPK/mobA/mobA-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006777 Mo-molybdopterin cofactor biosynthetic process | IEA GO_REF:0000002 | MODIFY | Summary: MobA participates in the nucleotide-maturation branch of Mo-molybdopterin cofactor biosynthesis. Reason: Correct but general. The earlier draft accepted the broad term to avoid asserting bis-MGD assembly, but the review already accepts the descendant GO:1902758 (bis-MGD biosynthesis, the TreeGrafter batch-05 verdict), and the E. coli ortholog's role in bis-MGD formation is experimental. The row is refined to GO:1902758, as in ECOLI/mobA. Proposed replacements: bis(molybdopterin guanine dinucleotide)molybdenum biosynthetic process Supporting Evidence: file:PSEPK/mobA/mobA-uniprot.txt CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) CC cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine CC dinucleotide (Mo-MGD) cofactor. {ECO:0000255|HAMAP-Rule:MF_00316}. |
| GO:0016779 nucleotidyltransferase activity | IEA GO_REF:0000120 | MODIFY | Summary: The generic nucleotidyltransferase term should be replaced by the exact MobA activity. Reason: UniProt specifies GMP transfer from GTP to Mo-MPT. Proposed replacements: molybdenum cofactor guanylyltransferase activity Supporting Evidence: file:PSEPK/mobA/mobA-uniprot.txt CC -!- CATALYTIC ACTIVITY: CC Reaction=Mo-molybdopterin + GTP + H(+) = Mo-molybdopterin guanine CC dinucleotide + diphosphate; Xref=Rhea:RHEA:34243, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71302, CC ChEBI:CHEBI:71310; EC=2.7.7.77; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00316}; |
| GO:0019720 Mo-molybdopterin cofactor metabolic process | IEA GO_REF:0000104 | MODIFY | Summary: This broad metabolic-process parent is less precise than the retained Mo-molybdopterin cofactor biosynthetic-process annotation. Reason: Correct but general, so MODIFY rather than the draft's MARK_AS_OVER_ANNOTATED. MobA works in the biosynthetic direction, specifically bis-MGD formation, which the review accepts as GO:1902758; same action as ECOLI/mobA. Proposed replacements: bis(molybdopterin guanine dinucleotide)molybdenum biosynthetic process Supporting Evidence: file:PSEPK/mobA/mobA-uniprot.txt CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) CC cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine CC dinucleotide (Mo-MGD) cofactor. {ECO:0000255|HAMAP-Rule:MF_00316}. |
| GO:0061603 molybdenum cofactor guanylyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This is the exact core molecular function of MobA. Reason: The reviewed entry provides Rhea:34243 and EC 2.7.7.77 for Mo-MPT guanylylation. Supporting Evidence: file:PSEPK/mobA/mobA-uniprot.txt CC -!- CATALYTIC ACTIVITY: CC Reaction=Mo-molybdopterin + GTP + H(+) = Mo-molybdopterin guanine CC dinucleotide + diphosphate; Xref=Rhea:RHEA:34243, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71302, CC ChEBI:CHEBI:71310; EC=2.7.7.77; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00316}; file:PSEPK/mobA/mobA-deep-research-openscientist.md GTP + Mo-MPT --(MobA, Mg2+)--> MGD + PPi |
| GO:0070568 guanylyltransferase activity | IEA GO_REF:0000104 | MODIFY | Summary: The broad guanylyltransferase term should be replaced by the Mo-cofactor-specific child term. Reason: The acceptor is specifically Mo-molybdopterin. Proposed replacements: molybdenum cofactor guanylyltransferase activity Supporting Evidence: file:PSEPK/mobA/mobA-uniprot.txt CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) CC cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine CC dinucleotide (Mo-MGD) cofactor. {ECO:0000255|HAMAP-Rule:MF_00316}. |
| GO:1902758 bis(molybdopterin guanine dinucleotide)molybdenum biosynthetic process | IEA GO_REF:0000118 | ACCEPT | Summary: MobA's guanylyl transfer is the step that builds the bis-MGD cofactor. Reason: The previous rejection read the single-MGD reaction equation as excluding the bis-MGD product, but bis-MGD is assembled by two successive MobA guanylyl transfers onto Mo-MPT, and the process term is how GO records that contribution: the characterised E. coli ortholog MobA (P32173) carries GO:1902758 with experimental IMP evidence (PMID:1648082) as well as an IBA at PANTHER:PTN001452269 in current GOA. Q88HA3 has the same EC 2.7.7.77 guanylyltransferase assignment and MobA family signature, so the propagated process term describes work this protein performs rather than a downstream event attributed to it. Supporting Evidence: file:PSEPK/mobA/mobA-uniprot.txt CC -!- CATALYTIC ACTIVITY: CC Reaction=Mo-molybdopterin + GTP + H(+) = Mo-molybdopterin guanine CC dinucleotide + diphosphate; Xref=Rhea:RHEA:34243, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71302, CC ChEBI:CHEBI:71310; EC=2.7.7.77; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00316}; |
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Download this section (compressed HTML)Experiment: Quantify Mo-MGD formation by purified Q88HA3 and test complementation of an MGD-dependent molybdoenzyme phenotype in a mobA deletion strain.
Type: enzyme assay and genetic complementation
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