Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1.
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phzS expressed alone converts PCA to 1-hydroxyphenazine, and phzM or phzS insertion mutants of P. aeruginosa lack pyocyanin.
"Expression of phzS alone in Escherichia coli or in enzymes, pyocyanin-nonproducing P. fluorescens resulted in conversion of PCA to 1-hydroxyphenazine."
The purification, crystallization and preliminary structural characterization of FAD-dependent monooxygenase PhzS, a phenazine-modifying enzyme from Pseudomonas aeruginosa.
Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa.
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Purified PhzS hydroxylates PCA to 1-hydroxyphenazine NADH-dependently (PCA is a poor, uncoupling substrate); PhzM plus PhzS make pyocyanin from PCA, which needs SAM, NADH and O2.
"There were indications however that PCA is a poor substrate for PhzS as complete conversion of PCA to 1-HP was not obtained and more NADH was consumed than the amount of 1-HP produced."
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PhzS is a monomer in solution, and no stable PhzM-PhzS complex was detected.
"indicating it is a monomer in solution"
Crystal structure of the pyocyanin biosynthetic protein PhzS.
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2.4 A structure of PhzS shows a p-hydroxybenzoate hydroxylase-type aromatic hydroxylase with FAD in the out conformation.
"The structure reveals that PhzS is a member of the family of aromatic hydroxylases characterized by p-hydroxybenzoate hydroxylase."
UniProt entry Q9HWG9 (PHZS_PSEAE)
Composition of PAINT node PTN002492679 (PTHR13789) and its leaf IBAs