Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Annotating enzymes of unknown function: N-formimino-L-glutamate deiminase is a member of the amidohydrolase superfamily.
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PA5106 deiminates FIGLU to N-formylglutamate and ammonia; PA5091 (HutG) hydrolyses N-formylglutamate; PA3175 (HutE) cleaves FIGLU directly.
"The protein Pa5106 was shown to catalyze the deimination of N-formimino-L-glutamate to ammonia and N-formyl-L-glutamate"
Mechanistic characterization of N-formimino-L-glutamate iminohydrolase from Pseudomonas aeruginosa.
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Purified HutF contains zinc, loses activity on chelation, and needs Glu235, His269 and Asp320 for catalysis.
"The purified enzyme contained up to one equivalent of zinc."
Formation and operation of the histidine-degrading pathway in Pseudomonas aeruginosa.
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Histidase, urocanase and FIGLU-degrading capacity (steps I, II and IV) are induced by urocanate and catabolite-repressed; FIGLU degradation is measured only as a pooled extract activity, and no hutF mutant is described.
"Histidine ammonia lyase (histidase), urocanase, and the capacity to degrade formiminoglutamate, which are respectively involved in steps I, II, and IV in the catabolism of histidine"
Structure of N-formimino-L-glutamate iminohydrolase from Pseudomonas aeruginosa.
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Crystal structures of PA5106 with inhibitors; single zinc coordinated by His56, His58, His232 and Asp320.
"The active site of Pa5106 contains a single zinc atom that is coordinated by His-56, His-58, His-232, and Asp-320."