Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase.
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A PMM-deficient algC mutant carries a single arginine-to-cysteine substitution near the C terminus.
"DNA sequence analysis of a defective algC gene (algC') cloned from a mutant of P. aeruginosa that lacked PMM activity revealed one point mutation"
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algC transcription is activated by AlgR.
"suggesting that the algR1 gene product activates the transcription of the algC gene"
Synthesis of multiple Pseudomonas aeruginosa biofilm matrix exopolysaccharides is post-transcriptionally regulated.
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AlgC is required for Psl and Pel as well as alginate and LPS precursors.
"Here we demonstrated that AlgC, a key enzyme that provides sugar precursors for the synthesis of alginate and lipopolysaccharides (LPS) is also required for both Psl and Pel production."
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AlgC is proposed to act as a checkpoint controlling the sugar precursor pool.
"we propose that AlgC is a key checkpoint enzyme that coordinates the total amount of exopolysaccharide biosynthesis by controlling sugar precursor pool"
Identification of an essential active-site residue in the α-D-phosphohexomutase enzyme superfamily.
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His329 is critical for catalysis and likely acts as the general base.
"His329 is appropriately positioned to abstract a proton from the O1/O6 hydroxyl of the phosphosugar substrates, and thus may serve as the general base in the reaction"
The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required for the synthesis of a complete lipopolysaccharide core.
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algC mutants lack PMM and PGM activity, and algC complements an E. coli pgm mutant.
"we transferred the cloned, intact P. aeruginosa algC gene to a pgm mutant of Escherichia coli and observed complementation of the pgm phenotype"
Purification and characterization of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa involved in biosynthesis of both alginate and lipopolysaccharide.
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Purified AlgC is a monomer with both PMM and PGM activity and a twofold preference for G1P by kcat/Km.
"The enzyme catalyzed the interconversion of mannose 1-phosphate (M1P) and mannose 6-phosphate, as well as that of glucose 1-phosphate (G1P) and glucose 6-phosphate."
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Minor activity on ribose 1-phosphate and 2-deoxyglucose 6-phosphate.
"PMM also catalyzed the conversion of ribose 1-phosphate and 2-deoxyglucose 6-phosphate to their corresponding isomers, although activities were much lower."
The Pseudomonas aeruginosa algC gene product participates in rhamnolipid biosynthesis.
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AlgC is required for rhamnolipid production, presumably by making glucose 1-phosphate for dTDP-L-rhamnose synthesis.
"presumably catalyzing the first step in the deoxy-thymidine-diphospho-L-rhamnose (dTDP-L-rhamnose) pathway, the conversion of glucose-6-phosphate to glucose-1-phosphate"
Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors.
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AlgC has four domains, three with a similar fold, all contributing to the active-site cleft.
"Residues from all four domains of the protein contribute to the formation of a large active site cleft in the center of the molecule."
Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.
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A single active site accommodates both glucose and mannose phosphosugars.
"The ability of PMM/PGM to accommodate these four diverse substrates in a single active site is consistent with its highly reversible phosphoryl transfer reaction and allows it to function in multiple biosynthetic pathways in P. aeruginosa."
Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.
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The reaction proceeds through a bisphosphorylated sugar intermediate that reorients in the active site.
"This phenomenon is consistent with a mechanism in which the enzyme phosphorylates the substrate to generate a bisphosphorylated intermediate that reorients in the active site to return its original phosphoryl group to the enzyme and generate the observed product."
The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme.
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The intermediate reorients without dissociating from the active site.
"Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is, thus, a simple example of processivity"
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.
Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa.
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AlgC contributes to alginate, LPS and rhamnolipid biosynthesis, and substrate binding closes domain 4 over the active site.
"is involved in the biosynthesis of several complex carbohydrates, including alginate, lipopolysaccharide, and rhamnolipid"
Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect.
UniProt record for algC (P26276)