Gene Ontology annotation through association of InterPro records with GO terms.
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods.
Mercuric reductase: homology to glutathione reductase and lipoamide dehydrogenase. Iodoacetamide alkylation and sequence of the active site peptide
NmerA, the metal binding domain of mercuric ion reductase, removes Hg2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions
C-terminal cysteines of Tn501 mercuric ion reductase.
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Site-directed mutagenesis proved C-terminal cysteines Cys558 and Cys559 are essential for mercury reduction activity
"Compared to wild-type enzyme, the C558A mutant shows a 20-fold reduction in kcat and a 10-fold increase in Km, for an overall decrease in catalytic efficiency of 200-fold in kcat/Km"
Bacterial mercury resistance from atoms to ecosystems
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Comprehensive review establishing merA as essential for mercury resistance across diverse bacteria
"Bacterial resistance to inorganic and organic mercury compounds (HgR) is one of the most widely observed phenotypes in eubacteria"
Mercury resistance and mercuric reductase activities and expression among chemotrophic thermophilic Aquificae.
Deep Research Report on merA gene
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MerA is a cytoplasmic enzyme that reduces Hg(II) to Hg(0) as part of bacterial mercury resistance
"MerA is a cytosolic enzyme, functioning within the bacterial cytoplasm to reduce mercury ions. When P. aeruginosa carrying a mer plasmid is induced with mercury, MerA can constitute up to ~6% of the soluble (cytoplasmic) protein content."
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MerA contains specialized structural features for mercury handling
"A unique structural feature of MerA is the additional C-terminal cysteine pair (e.g., Cys558 and Cys559) which is not found in most other flavoprotein reductases. These residues form a flexible loop that transiently coordinates the Hg²⁺ ion."