Gene Ontology annotation through association of InterPro records with GO terms
TreeGrafter-generated GO annotations
Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp.
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NADPH-specific malonyl-CoA reductase activity in M. sedula is induced about 10-fold under autotrophic growth. The enzyme was identified via N-terminal sequencing and characterized as recombinant S. tokodaii ortholog.
"Extracts of Metallosphaera sedula contained NADPH-specific malonyl-CoA reductase activity that was 10-fold up-regulated under autotrophic growth conditions."
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MCR is an ASD paralog, unrelated to the Chloroflexus enzyme.
"Malonyl-CoA reductase has 38% amino acid sequence identity to aspartate-semialdehyde dehydrogenase, suggesting a common ancestor for both proteins."
A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea.
The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism.
Malonic semialdehyde reductase, succinic semialdehyde reductase, and succinyl-coenzyme A reductase from Metallosphaera sedula: enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in Sulfolobales.
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The succinyl-CoA reductase purified from autotrophic M. sedula was identified as Msed_0709, so MCR is a promiscuous malonyl-CoA/succinyl-CoA reductase.
"Interestingly, succinyl-CoA reductase turned out to be identical to malonyl-CoA reductase."
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Near-equal activity with both substrates.
"These data showed that malonyl-CoA reductase is a promiscuous enzyme and acts nearly equally well with malonyl-CoA and succinyl-CoA."
Structural basis for a bispecific NADP+ and CoA binding site in an archaeal malonyl-coenzyme A reductase.
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Crystal structures of the S. tokodaii ortholog show a homotetramer with a bispecific NADP+/CoA site and a remodelled ASD-derived substrate pocket.
"Structural analysis revealed an unexpected reaction cycle in which NADP + and CoA successively occupy identical binding sites."
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The mcr and asd paralogs are distinct genes in different genomic contexts.
"The two paralogous MCR and ASD enzymes show ∼40% amino acid sequence identity in the same organism, and their genes mcr and asd have different chromosomal locations."
Exploiting microbial hyperthermophilicity to produce an industrial chemical, using hydrogen and carbon dioxide.
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Msed_0709 (E2) was expressed in Pyrococcus furiosus as part of a partial 3HP/4HB cycle that produces 3-hydroxypropionate from CO2.
"E2 (malonyl/succinyl-CoA reductase, Msed_0709)"
UniProt record A4YEN2 (MCR_METS5)