Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The identification of an integral membrane, cytochrome c urate oxidase completes the catalytic repertoire of a therapeutic enzyme.
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Zebrafish Uox restores urate degradation in an Agrobacterium mutant lacking its urate oxidase.
"the phenotype was fully restored by complementation with a cytosolic Uox from zebrafish."
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Urate oxidation by zebrafish Uox generates H2O2, raising catalase four-fold.
"Consistent with H2O2 production by zfUox, urate oxidation in the complemented strain caused a four-fold increase of catalase."
Catalysis and Structure of Zebrafish Urate Oxidase Provide Insights into the Origin of Hyperuricemia in Hominoids.
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Uox catalyses the first reaction of the three-step oxidative uricolysis pathway.
"Urate oxidase (Uox) catalyses the first reaction of oxidative uricolysis, a"
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Zebrafish Uox is 298 aa with a C-terminal ARM tripeptide that is a type 1 peroxisome-targeting signal.
"encodes a protein of 298 aa with a C-terminal tripetide (ARM) corresponding to the type 1 peroxisome-targeting signal"
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Purified zebrafish Uox is predominantly tetrameric.
"with a large prevalence of the tetrameric assembly for both proteins"
A Trivalent Enzymatic System for Uricolytic Therapy of HPRT Deficiency and Lesch-Nyhan Disease.
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Zebrafish Uox, Urah and Urad were produced recombinantly as the uricolytic enzyme complement.
"We produced in recombinant form three zebrafish enzymes required in the uricolytic pathway."
Uricase-Deficient Larval Zebrafish with Elevated Urate Levels Demonstrate Suppressed Acute Inflammatory Response to Monosodium Urate Crystals and Prolonged Crystal Persistence.
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uox knockout larvae have reduced hepatic uox expression and elevated urate.
"We show that uox KO (uox−/−) larvae have significantly reduced expression of uox in the liver and elevated urate levels at early larval stages."
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The uox null mutant is a hyperuricemic larval model that remains viable.
"Here we describe a zebrafish uox null mutant that possesses elevated urate levels at larval stages."
UniProtKB entry Q6DG85 for Danio rerio uox
Falcon (Edison Scientific Literature) deep research report for Danio rerio uox (Q6DG85)
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Falcon synthesizes that zebrafish Uox is a classical cofactorless urate oxidase catalyzing oxidation/hydroxylation of urate to 5-hydroxyisourate (HIU).
"Zebrafish Uox catalyzes **oxidation/hydroxylation of urate to HIU**, and is described as the **classical cofactorless Uox** (i.e., it does not require a tightly bound organic cofactor)."
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Falcon places Uox among peroxisomal oxidases that use molecular oxygen as electron acceptor and generate hydrogen peroxide as a byproduct.
"Uox is grouped among peroxisomal oxidases that use **molecular oxygen (O₂)** as electron acceptor and generate **hydrogen peroxide (H₂O₂)** as a byproduct of oxidation chemistry"
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Falcon assigns Uox the first, rate-limiting step of the three-step uricolysis pathway, followed by Urah (HIU hydrolase) and Urad (OHCU decarboxylase) to (S)-allantoin.
"the canonical uricolysis pathway is a **three-enzyme** sequence in which Uox generates **5-hydroxyisourate (HIU)**, followed by HIU hydrolase (Urah) and OHCU decarboxylase (Urad) to yield **(S)-allantoin**."
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Falcon supports peroxisomal matrix localization of Uox via a C-terminal PTS1 (ARM) targeting signal and a zebrafish peroxisomal proteome inventory.
"DrUox encodes a C-terminal **ARM** tripeptide corresponding to a **PTS1** motif, indicating peroxisomal matrix import."
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Falcon reports the kinetic parameters of recombinant wild-type DrUox (Km ~11 uM, kcat ~4 per s) consistent with the UniProt KM value.
"**Wild-type DrUox:** **Km = 11 ± 1 μM**, **kcat ≈ 4 s⁻¹**."
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Falcon notes the homotetrameric T-fold architecture of zebrafish Uox with active sites at subunit interfaces.
"Zebrafish Uox forms a **tetramer** with the **T-fold** architecture typical of classical uricases; the functional active sites occur at subunit interfaces."