Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
ThrH, a homoserine kinase isozyme with in vivo phosphoserine phosphatase activity in Pseudomonas aeruginosa.
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thrB single mutants are prototrophic; thrB thrH double mutants are threonine auxotrophs. No ThrB enzyme assay is described in the abstract.
"In P. aeruginosa, threonine auxotrophy is observed only when both thrB and thrH are simultaneously inactivated."
Isolation, organization and expression of the Pseudomonas aeruginosa threonine genes.
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thrB cloned; its product resembles no known ThrB; insertional inactivation alone gives no phenotype, implying an isozyme.
"No phenotype could be detected when the chromosomal thrB gene was inactivated by an insertion."
The thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine:homoserine phosphotransferase activity.
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ThrH, the thrB-redundant partner, is a phosphoserine phosphatase that transfers phosphate from phosphoserine to homoserine, not an ATP-dependent kinase.
"ThrH has a novel phosphoserine:homoserine phosphotransferase activity"
Ultrahigh-throughput functional profiling of microbiota communities.
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B. subtilis YerI (AmiN homolog, a PTN001464661 leaf) phosphorylates amicoumacin A and mediates resistance.
"B. subtilis 168 has an amiN homolog (yerI) that also phosphorylates Ami, mediating natural B. subtilis resistance to the drug."