Literature summary for 1.14.13.195 extracted from

Imperi, F.; Putignani, L.; Tiburzi, F.; Ambrosi, C.; Cipollone, R.; Ascenzi, P.; Visca, P.
Membrane-association determinants of the omega-amino acid monooxygenase PvdA, a pyoverdine biosynthetic enzyme from Pseudomonas aeruginosa (2008), Microbiology, 154, 2804-2813.

Search for more literature for 1.14.13.195

Cloned(Commentary)

Cloned (Comment)	Organism
expression of PvdA-PhoA fusion protein mutants in Escherichia coli strain LMG194	Pseudomonas aeruginosa

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of PvdA-PhoA fusion protein mutantsa nd of a pvdA deletion mutant strain	Pseudomonas aeruginosa

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
inner membrane	the enzyme anchors in the inner membrane with its N-terminus, while the bulk of the enzyme is located in the cytosol, the transmembrane region overlaps the FAd binding site, membrane-association determinants of PvdA and analysis of membrane topology, overview	Pseudomonas aeruginosa	-	-

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	gene pvdA	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
flavoprotein	-	Pseudomonas aeruginosa

Subunits

Subunits	Comment	Organism
More	PvdA secondary structure and transmembrane region, overview	Pseudomonas aeruginosa

Synonyms

Synonyms	Comment	Organism
omega-amino acid monooxygenase	-	Pseudomonas aeruginosa
PvdA	-	Pseudomonas aeruginosa

Cofactor

Cofactor	Comment	Organism	Structure
FAD	binding motif, overview	Pseudomonas aeruginosa
NADPH	binding motif, overview	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)