Gene Ontology annotation through association of InterPro records with GO terms
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales.
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The dehydratase was purified from M. sedula and identified as Msed_2001.
"The best hit was the Msed_2001 gene annotated as an enoyl-CoA hydratase gene (100% identity and 41% coverage) coding for a 28.3-kDa (259 amino acids) protein."
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The enzyme also hydrates crotonyl-CoA, with (S) stereospecificity, at a rate similar to that with 3-hydroxypropionyl-CoA.
"3-Hydroxypropionyl-CoA dehydratase acted nearly equally as well on ( S )-3-hydroxybutyryl-CoA as on 3-hydroxypropionyl-CoA."
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Activity is not reduced in heterotrophically grown cells.
"was not downregulated in heterotrophically grown cells"
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The monomeric state reported here from gel filtration may be an underestimate.
"This experimental value may be underestimated due to the very small amounts of enzyme used."
Convergent Evolution of a Promiscuous 3-Hydroxypropionyl-CoA Dehydratase/Crotonyl-CoA Hydratase in Crenarchaeota and Thaumarchaeota.
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Msed_2001 performs both the 3-hydroxypropionyl-CoA dehydratase and the crotonyl-CoA hydratase reactions of the cycle in vivo. It is the most abundant of the six M. sedula crotonase homologs.
"Msed_2001 is responsible for 99% of 3-hydroxypropionyl-CoA dehydratase activity and for 86% of crotonyl-CoA hydratase activity in M. sedula"
Structural Insight into Substrate Specificity of 3-Hydroxypropionyl-Coenzyme A Dehydratase from Metallosphaera sedula.
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Crystal structure with CoA (PDB 5ZAI). The small enoyl pocket suits short-chain substrates, and the enzyme is a hexamer in solution.
"Size-exclusion chromatography confirmed that the enzymes also exists as a hexamer in solution (Fig. 2c)."
Reaction kinetic analysis of the 3-hydroxypropionate/4-hydroxybutyrate CO(2) fixation cycle in extremely thermoacidophilic archaea.
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Recombinant HPCD (Msed_2001) is active and forms an octamer. It may associate weakly with 3-hydroxypropionyl-CoA synthetase.
"Recombinant HPCD formed a homo-octamer, with an estimated molecular mass of 220 kDa"
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Possible HPCS-HPCD interaction.
"Thus, a weak association between HPCS and HPCD is plausible and may be representative of a larger metabolon involving some or all of the 3HP/4HB cycle enzymes."
Enzymes Catalyzing Crotonyl-CoA Conversion to Acetoacetyl-CoA During the Autotrophic CO(2) Fixation in Metallosphaera sedula.
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Other M. sedula crotonase homologs have only low 3-hydroxypropionyl-CoA dehydratase activity.
"The studied crotonases are homologous to 3-hydroxypropionyl-CoA dehydratase Msed_2001 and possess low 3-hydroxypropionyl-CoA dehydratase activity"
A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea.
A TetR-family transcription factor regulates fatty acid metabolism in the archaeal model organism Sulfolobus acidocaldarius.
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In S. acidocaldarius, beta-oxidation enzymes are encoded in a dedicated FadR-regulated gene cluster.
"acting as a repressor of a 30-kb gene cluster comprising 23 open reading frames encoding lipases and β-oxidation enzymes."