Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Unveiling the genes responsible for the unique Pseudomonas aeruginosa oleate-diol synthase activity.
-
PA2077 encodes the 10S-dioxygenase that performs the first step of oleate-diol synthesis.
"gene PA2077 codes for the 10S-dioxygenase activity (10S-DOX) responsible for the first step of the reaction"
-
PA2077 and PA2078 act separately, without forming a complex.
"Heterologous expression of both enzymes separately showed that no hetero-complex formation is required for enzymatic activity."
In Silico/In Vivo Insights into the Functional and Evolutionary Pathway of Pseudomonas aeruginosa Oleate-Diol Synthase. Discovery of a New Bacterial Di-Heme Cytochrome C Peroxidase Subfamily.
-
Both heme sites of PA2077 are required for dioxygenase activity.
"Mutants at either position H130 or H375 (residue numbering with signal peptide) in protein PA2077 failed to convert oleic acid into 10-H(P)OME (Fig 5), definitely showing that both histidines (the two hemes) are required by PA2077 to display activity."
-
PA2077 and PA2078 are periplasmic.
"both proteins display type I signal export sequences that allow transport of the synthesized products to the periplasm, a fact experimentally confirmed by PhoA fusion screening"
-
The pair are in-paralogs with very low homology outside Pseudomonas orthologues.
"PA2077 and PA2078 display very low homology to other proteins in the databases, except for those corresponding to their orthologues in other P."
-
The pair lie outside the branch of characterized cytochrome c peroxidases.
"Nevertheless, the phylogenetic results obtained here indicate that PA2077 and PA2078 do not group in the main phylogenetic branch described so far for functionally characterized Ccps, constituting thus a new cluster of functional and structural enzymes."