guaD

UniProt ID: Q88F18
Organism: Pseudomonas putida KT2440
Review Status: COMPLETE
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Gene Description

GuaD is the predicted zinc-dependent guanine deaminase that hydrolytically converts guanine to xanthine and ammonium, supplying xanthine to downstream purine-base oxidation. The exact KT2440 protein has not been characterized biochemically; its assignment is supported by the diagnostic guanine-deaminase family classification, conserved reaction annotation, and PANTHER phylogenetic propagation from characterized orthologs.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0005829 cytosol
IEA
GO_REF:0000118
KEEP AS NON CORE
Summary: TreeGrafter predicts a soluble cytosolic location for GuaD.
Reason: A cytosolic location is compatible with purine-base metabolism, but it is an inferred family-level localization and does not define the enzyme's core function. The TreeGrafter row rests on the PTHR11271 PAINT cytosol node, and Q88F18 is a soluble protein with no predicted signal peptide or transmembrane segment, so the inherited location is plausible.
Supporting Evidence:
file:interpro/panther/PTHR11271/PTHR11271-paint.tsv
PTHR11271 PTN000138454 GO:0005829 C IBD false
file:PSEPK/guaD/guaD-uniprot.txt
FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
GO:0006147 guanine catabolic process
IEA
GO_REF:0000120
ACCEPT
Summary: GuaD consumes guanine in the single deamination step that produces xanthine.
Reason: This is the immediate biological process of the predicted guanine deaminase reaction.
Supporting Evidence:
file:PSEPK/guaD/guaD-uniprot.txt
PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
file:interpro/panther/PTHR11271/PTHR11271-paint.tsv
PTHR11271 PTN000138455 GO:0006147
GO:0008270 zinc ion binding
IEA
GO_REF:0000120
KEEP AS NON CORE
Summary: The guanine-deaminase family is predicted to use one catalytic zinc ion per subunit.
Reason: Zinc binding is a credible catalytic cofactor property but is ancillary to the exact guanine deaminase activity. GOA names PTN002259155 in WITH/FROM; the cached family PAINT slice independently records the same term at the experimentally seeded IBD node PTN000138455.
Supporting Evidence:
file:PSEPK/guaD/guaD-uniprot.txt
Note=Binds 1 zinc ion per subunit.
file:interpro/panther/PTHR11271/PTHR11271-paint.tsv
PTHR11271 PTN000138455 GO:0008270
GO:0008892 guanine deaminase activity
IEA
GO_REF:0000120
ACCEPT
Summary: GuaD is predicted to catalyze guanine hydrolysis to xanthine and ammonium.
Reason: The exact reaction, diagnostic InterPro family, and PANTHER node propagated from experimentally annotated orthologs converge on guanine deaminase activity. GOA names PTN002259155 in WITH/FROM, while the cached family PAINT slice independently records the term at IBD node PTN000138455. No direct enzymology has been reported for Q88F18 itself.
Supporting Evidence:
file:PSEPK/guaD/guaD-uniprot.txt
Reaction=guanine + H2O + H(+) = xanthine + NH4(+);
file:interpro/panther/PTHR11271/PTHR11271-paint.tsv
PTHR11271 PTN000138455 GO:0008892
file:PSEPK/guaD/guaD-deep-research-openscientist.md
The gene **guaD** (ordered locus **PP_4281**; UniProt **Q88F18**) of *Pseudomonas putida* strain KT2440 encodes **guanine deaminase** (guanase; EC 3.5.4.3)
GO:0016787 hydrolase activity
IEA
GO_REF:0000002
TOO GENERAL
Summary: This broad parent is true but adds no information beyond guanine deaminase activity.
Reason: GO:0008892 guanine deaminase activity is_a GO:0016787 hydrolase activity, and the specific child is accepted on another row of this review, so the generic catalytic class is true but uninformative.
Supporting Evidence:
file:PSEPK/guaD/guaD-uniprot.txt
Reaction=guanine + H2O + H(+) = xanthine + NH4(+);
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
IEA
GO_REF:0000002
TOO GENERAL
Summary: This parent class is entailed by the exact guanine deaminase reaction.
Reason: GO:0008892 guanine deaminase activity is_a this carbon-nitrogen hydrolase class, and the specific child is accepted on another row of this review, so the term is true but uninformative.
Supporting Evidence:
file:PSEPK/guaD/guaD-uniprot.txt
Reaction=guanine + H2O + H(+) = xanthine + NH4(+);
GO:0019239 deaminase activity
IEA
GO_REF:0000118
TOO GENERAL
Summary: True is_a ancestor of guanine deaminase activity.
Reason: GO:0008892 guanine deaminase activity is_a GO:0019239 in the current ontology, so the broad term correctly describes the hydrolytic deamination (guanine + H2O = xanthine + NH4+, EC 3.5.4.3) assigned to Q88F18's guanine-deaminase family. The claim is true, not an over-annotation; it is uninformative because the accepted child term on another row of this review entails it.
Supporting Evidence:
file:interpro/panther/PTHR11271/PTHR11271-paint.tsv
PTHR11271 PTN000138454 GO:0019239 F IBD false
file:PSEPK/guaD/guaD-uniprot.txt
Reaction=guanine + H2O + H(+) = xanthine + NH4(+);
GO:0046098 guanine metabolic process
IEA
GO_REF:0000118
TOO GENERAL
Summary: True is_a ancestor of guanine catabolic process.
Reason: GO:0006147 guanine catabolic process is_a GO:0046098 guanine metabolic process, so the propagated parent is true of GuaD's reaction. It is not an over-annotation; it is uninformative because the accepted child term on the UniRule row of this review entails it.
Supporting Evidence:
file:interpro/panther/PTHR11271/PTHR11271-paint.tsv
PTHR11271 PTN000138455 GO:0006147 P IBD false
file:PSEPK/guaD/guaD-uniprot.txt
PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:

Core Functions

Zinc-dependent guanine deaminase predicted to hydrolyze guanine to xanthine and ammonium, providing xanthine for downstream purine-base oxidation.

Molecular Function:
guanine deaminase activity
Directly Involved In:
Supporting Evidence:
  • file:PSEPK/guaD/guaD-uniprot.txt
    Reaction=guanine + H2O + H(+) = xanthine + NH4(+);
  • file:interpro/panther/PTHR11271/PTHR11271-paint.tsv
    PTHR11271 PTN000138455 GO:0008892
  • file:PSEPK/guaD/guaD-deep-research-openscientist.md
    No direct enzymology on the KT2440 protein.

References

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Suggested Questions for Experts

Q: Does purified Q88F18 preferentially deaminate guanine under physiologically relevant conditions in KT2440?

Suggested experts: bacterial purine-catabolism experts

Suggested Experiments

Experiment: Purify Q88F18 and measure zinc-dependent steady-state kinetics for guanine, including a limited alternative-substrate panel to distinguish its primary reaction from possible promiscuous activities.

Type: enzyme activity assay

Deep Research

OpenScientist

(guaD-deep-research-openscientist.md)

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πŸ“š Additional Documentation

Notes

(guaD-notes.md)

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