Literature summary for 2.7.7.75 extracted from

Kanaujia, S.P.; Jeyakanthan, J.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.; Sekar, K.
Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organisms (2011), Acta Crystallogr. Sect. F, 67, 2-16.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli as a His-tagged fusion protein	Aquifex aeolicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of AaMogA is determined at 1.7 A resolution (space group P2 resolution), or 1.9 A resolution (space group P1)	Aquifex aeolicus

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	Q5SLF2	-	-

Purification (Commentary)

Purification (Comment)	Organism
using Ni-NTA chromatography	Aquifex aeolicus

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + H2Dtpp-mP = diphosphate + H2Dtpp-mADP	comparative analyses reveal a possible role for the N- and C-terminal residues of MoaB and MogA proteins, respectively, in stabilizing the substrate and/or product molecule in the active site	Aquifex aeolicus	a

Subunits

Subunits	Comment	Organism
oligomer	-	Aquifex aeolicus

Synonyms

Synonyms	Comment	Organism
AaMogA	-	Aquifex aeolicus

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Release 2023.1 (January 2023)