Uricase is an oxidoreductase enzyme that plays a specific role in the process of purine metabolism, especially in degrading uric acid into water-soluble compounds, they are allantoin, CO2, and H2O2. Some sources of uricase include microorganisms, higher plants, and animals, except humans. Bacillus altitudinis strain W.IIISRNs_1.1 from the hot spring of Mataumpana is the focus of this work, which works to produce and characterize the uricase enzyme from this novel isolate. The clear zone formed around a colony after being cultured at 45oC in a solid Glucose Yeast Peptone (GYP) medium containing 0.2 % of uric acid shows bacteria's capacity to digest uric acid. The morphological and physiological identification of strain W.IIISRNs_1.1 is a group of bacteria from Bacillus genus, and 16S rRNA analysis identified strain W.IIISRNs_1.1 as Bacillus altitudinis. The result of this study shows that the optimum optical density was 1.17 (60 hours of incubation), which was not following the incubation time for the optimum production of the uricase enzyme, which was 36 hours with enzyme activity 0.5198 U/mL and protein concentration of 1.2819 mg/mL. Uricase from Bacillus altitudinis strain W.IIISRNs_1.1 best produced with substrate concentration 0.2% of uric acid, worked optimally at 45ºC and pH 8, stable at 45ºC for 2.5 hours, pH 8 and 9 for 1.5 hours. The maximum speed of uricase enzyme work occurred at the substrate concentration (uric acid) 3.5 mM. The uricase enzyme is activated by several metal ions, namely Ca2+, K+, and Ba2+ with a concentration of 0.1 M. Enzymes were significantly inhibited by 0.1 M Zn2+, Co2+, and 0.05 mM Na+, Zn2+ ions. Uricase from Bacillus altitudinis strain W.IIISRNs_1.1 is a uric acid degrading enzyme from a novel source and has not been produced before. This enzyme is potential to be developed in biochemical and clinical applications.