Gene Ontology annotation through association of InterPro records with GO terms
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Identification of missing genes and enzymes for autotrophic carbon fixation in crenarchaeota.
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Msed_0399 was purified from autotrophically grown M. sedula as the bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutyryl-CoA dehydrogenase and identified by mass spectrometry.
"Mass-spectrometric analysis identified the 70-kDa protein as Msed_0399."
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The recombinant enzyme uses NAD+, not NADP+, and is specific for the (S) stereoisomer.
"NADP + , acryloyl-CoA, 3-hydroxypropionyl-CoA, and the ( R ) stereoisomer of 3-hydroxybutyryl-CoA were not transformed."
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The protein is a fusion of an N-terminal dehydrogenase and a C-terminal enoyl-CoA hydratase.
"an apparent fusion protein (∼70 kDa) of an enoyl-CoA hydratase (C-terminal domain, ∼20 kDa) and a dehydrogenase (N-terminal domain, ∼40 kDa)"
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The activity is not autotrophy-specific.
"The expected bifunctional hydratase/dehydrogenase activity was present in similar amounts in extracts of autotrophically and heterotrophically grown cells of M. sedula"
Conversion of 4-hydroxybutyrate to acetyl coenzyme A and its anapleurosis in the Metallosphaera sedula 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway.
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Recombinant Msed_0399, with Msed_0406, Msed_1321 and Msed_0656, converts 4-hydroxybutyrate to acetyl-CoA in vitro with NAD+.
"were produced recombinantly in Escherichia coli , combined in vitro , and shown to convert 4HB to acetyl-CoA."
Enzymes Catalyzing Crotonyl-CoA Conversion to Acetoacetyl-CoA During the Autotrophic CO(2) Fixation in Metallosphaera sedula.
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Msed_1423, not Msed_0399, is the main (S)-3-hydroxybutyryl-CoA dehydrogenase of the cycle in Sulfolobales.
"show that Msed_1423 is the main (S)-3-hydroxybutyryl-CoA dehydrogenase in the HP/HB cycle in Sulfolobales."
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The Msed_0399 gene is absent from several autotrophic Sulfolobales.
"This is corroborated by the fact that its gene is absent in many other autotrophic Sulfolobales."
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Both activities act on C8 substrates, and the hydratase is most active on octenoyl-CoA.
"Similarly, it acted as dehydrogenase with both C4 and C8 (S)-3-hydroxyacyl-CoAs (Table 2)."
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The gene lies in a beta-oxidation-like gene cluster.
"In fact, msed_0399 is located in the cluster with the genes homologous to various β-oxidation genes (Figure 2A)"
Convergent Evolution of a Promiscuous 3-Hydroxypropionyl-CoA Dehydratase/Crotonyl-CoA Hydratase in Crenarchaeota and Thaumarchaeota.
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Msed_0399 contributes about 8% of the crotonyl-CoA hydratase activity of autotrophic M. sedula. Msed_2001 supplies about 86%.
"the latter probably with some contribution of Msed_0399 (8.2%)"
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Msed_0399 carries at most a small flux in the cycle.
"Msed_0399, which was previously thought to be responsible for crotonyl-CoA conversion into acetoacetyl-CoA, is responsible for a small flux in autotrophically grown M. sedula, at best."
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 gene cluster regulated by FadR.
"acting as a repressor of a 30-kb gene cluster comprising 23 open reading frames encoding lipases and β-oxidation enzymes."
UniProt entry A4YDS4
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The ARBA SIMILARITY line places the crotonase in the N-terminal section, which contradicts the entry's own Pfam domain coordinates (crotonase at 407-650) and PMID:21169482.
"In the N-terminal section; belongs to the enoyl-CoA"