moaB-I

UniProt ID: Q88L15
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

moaB-I encodes a soluble MoaB-family protein adjacent to moeA. 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.

Existing Annotations Review

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: Q88L15 lacks membrane/export features and is adjacent to cytosolic moeA.
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 Q88L15's role.
Supporting Evidence:
file:PSEPK/moaB-I/moaB-I-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-I/moaB-I-deep-research-openscientist.md
2. **MoaB's precise physiological role is unresolved even in *E. coli*.** Despite two crystal structures, the specific in vivo activity of MoaB (as distinct from MogA) has never been unambiguously established.

Core Functions

MoaB-family GTP/MPT-binding protein with an unresolved catalytic or accessory contribution to molybdenum-cofactor biosynthesis.

Supporting Evidence:
  • file:PSEPK/moaB-I/moaB-I-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-I/moaB-I-deep-research-openscientist.md
    4. **Substrate specificity is inferred, not measured.** The predicted substrate (molybdopterin) and product (MPT-AMP) derive from the Cnx1 and MogA literature, not from assays on MoaB-I.

References

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Suggested Questions for Experts

Q: Does Q88L15 catalyze MPT adenylylation, act as a noncatalytic partner of MoeA, or have no required role in KT2440 Mo-cofactor biosynthesis?

Suggested Experiments

Experiment: Compare purified Q88L15 with Q88E67 in MPT-binding, ATP-dependent MPT adenylylation, and MoeA-coupled Mo-MPT formation assays.

Type: comparative biochemical assay

Deep Research

OpenScientist

(moaB-I-deep-research-openscientist.md)

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