Gene Ontology annotation through association of InterPro records with GO terms
Epimerase (Msed_0639) and mutase (Msed_0638 and Msed_2055) convert (S)-methylmalonyl-coenzyme A (CoA) to succinyl-CoA in the Metallosphaera sedula 3-hydroxypropionate/4-hydroxybutyrate cycle.
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Msed_2055 encodes the coenzyme B12-binding MCM-beta subunit, encoded remotely from the catalytic MCM-alpha gene Msed_0638.
"the gene for the coenzyme B(12)-binding subunit of MCM (MCM-β) is located remotely (Msed_2055)"
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Active MCM requires coexpression of both subunits and is an alpha2beta2 heterotetramer.
"soluble, active MCM was produced only if MCM-α and MCM-β were coexpressed"
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MCM-beta carries the conserved B12-binding motif.
"The conserved coenzyme B(12)-binding motif (DXHXXG-SXL-GG) was identified in M. sedula MCM-β."
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Msed_2055 is transcriptionally induced under autotrophic growth.
"The expression of all three genes was significantly upregulated under autotrophic compared to heterotrophic growth conditions, implying a role in CO(2) fixation."
Identification of missing genes and enzymes for autotrophic carbon fixation in crenarchaeota.
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Genomic assignment of Msed_2055 as the small MCM subunit, overlapping the ArgK-like gene Msed_2056.
"Msed_2056 (ArgK-like) overlaps with the ORF encoding the small MCM subunit (cobalamin B12-binding domain protein Msed_2055), indicating the potential for cotranscription"
Novel B(12)-dependent acyl-CoA mutases and their biotechnological potential.
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The M. sedula MCM has a split organization, with a separate subunit homologous to the AdoCbl-binding domain of canonical MCM.
"A variant arrangement has been reported for MCM from Metallosphaera sedula that exhibits a split organization (Fig. 2) with one subunit being homologous to the substrate-binding domain and the second, to the AdoCbl-binding domain in the α-subunit of the canonical MCM"
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In class I B12-binding domains the DXHXXG histidine is the axial ligand to cobalt.
"in which the side chain of the histidine in a conserved DXHXXG motif, serves as the axial ligand to cobalt"
A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea.
UniProt record A4YIE3 (A4YIE3_METS5)
Msed_2055 B12-binding motif scan