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
3-Hydroxypropionyl-coenzyme A synthetase from Metallosphaera sedula, an enzyme involved in autotrophic CO2 fixation.
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Native M. sedula 3-hydroxypropionyl-CoA synthetase catalyses AMP-forming activation of 3-hydroxypropionate and is a homotetramer.
"3-Hydroxypropionyl-CoA synthetase, therefore, exists as a homotetramer."
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The enzyme is specific for 3-hydroxypropionate and propionate; acetate and butyrate are poor substrates owing to low affinity.
"The enzyme, therefore, is specific for 3-hydroxypropionate and propionate."
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The gene was identified as Msed_1456 (YP_001191537) from an internal peptide.
"Based on the internal peptide sequence determined for purified 3-hydroxypropionyl-CoA synthetase, a gene was identified in the genome of M. sedula which codes for a protein with an internal sequence that is a 100% match for the determined peptide sequence."
A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea.
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Defines the archaeal 3HP/4HB cycle, in which acetyl-CoA is regenerated via 4-hydroxybutyrate rather than malyl-CoA cleavage.
"This intermediate was reduced to 4-hydroxybutyrate and converted into two acetyl-CoA molecules via 4-hydroxybutyryl-CoA dehydratase."
Role of 4-hydroxybutyrate-CoA synthetase in the CO2 fixation cycle in thermoacidophilic archaea.
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Msed_1456 has equal activity on propionate and 3HP. The acetate/propionate synthetase of M. sedula is the separate paralog Msed_1353.
"Msed_1353 was active on propionate and acetate, but not on 4HB."
Reaction kinetic analysis of the 3-hydroxypropionate/4-hydroxybutyrate CO(2) fixation cycle in extremely thermoacidophilic archaea.
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Recombinant M. sedula HPCS (Msed_1456) is soluble and active only when co-expressed with HPCD (Msed_2001), and the two interact in yeast two-hybrid.
"Only when both enzymes were co-expressed in E. coli could HPCS be obtained in soluble, active form"
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Yeast two-hybrid interaction between HPCS and HPCD.
"The results demonstrate that HPCS and HPCD interact in vivo in yeast, although there is no evidence of interaction between ACR and SSR (Figure 2)."