Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Formation and operation of the histidine-degrading pathway in Pseudomonas aeruginosa.
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P. aeruginosa histidase was assayed and partially purified (MW about 210,000; Km for histidine 2 mM), and is induced by urocanate.
"The molecular weight of partially purified histidase was estimated at 210,000 by sucrose gradient centrifugation."
Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile.
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The P. putida histidase (82% identical to PA5098) is a homotetramer whose MIO electrophile forms from Ala-Ser-Gly 142-144.
"the reactive electrophile is a 4-methylidene-imidazole-5-one, which is formed autocatalytically by cyclization and dehydration of residues 142-144 with the sequence Ala-Ser-Gly"
Genetic analysis of the histidine utilization (hut) genes in Pseudomonas fluorescens SBW25.
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In P. fluorescens SBW25 only hutH2 (MIO-containing) is a functional histidase; hutH1 lacks the Ala-Ser-Gly active-site residues and is dispensable.
"deletion of hutH 1 had no effect; however, deletion of hutH 2 resulted in a strain unable to grow on histidine."
Annotating enzymes of unknown function: N-formimino-L-glutamate deiminase is a member of the amidohydrolase superfamily.
Induction of histidine-degrading enzymes in Pseudomonas aeruginosa.
Global regulation and virulence mediated by the histidine-responsive local transcription factor HutC in Pseudomonas aeruginosa.