Literature summary for 4.1.1.98 extracted from

Do, H.; Kim, S.; Lee, C.; Kim, H.; Park, H.; Kim, H.; Park, H.; Park, H.; Lee, J.
Crystal structure of UbiX, an aromatic acid decarboxylase from the psychrophilic bacterium Colwellia psychrerythraea that undergoes FMN-induced conformational changes (2015), Sci. Rep., 5, 8196 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of an FMN-bound wild type form and an FMN-unbound V47S mutant form. UbiX is a dodecameric enzyme, and each monomer possesses a typical Rossmann-fold structure. The FMN-binding domain of UbiX is composed of three neighboring subunits. The highly conserved Gly15, Ser41, Val47, and Tyr171 residues play important roles in FMN binding. The FMN-bound wild type form and the FMN-free form show a significant conformational difference in the C-terminal loop region (comprising residues 170-176 and 195-206)	Colwellia psychrerythraea

Crystallization (Comment)

Organism

structures of an FMN-bound wild type form and an FMN-unbound V47S mutant form. UbiX is a dodecameric enzyme, and each monomer possesses a typical Rossmann-fold structure. The FMN-binding domain of UbiX is composed of three neighboring subunits. The highly conserved Gly15, Ser41, Val47, and Tyr171 residues play important roles in FMN binding. The FMN-bound wild type form and the FMN-free form show a significant conformational difference in the C-terminal loop region (comprising residues 170-176 and 195-206)

Colwellia psychrerythraea

Protein Variants

Protein Variants	Comment	Organism
V47S	complete loss in FMN binding, crystal structure	Colwellia psychrerythraea

Organism

Organism	UniProt	Comment	Textmining
Colwellia psychrerythraea	Q489U8	-	-

Synonyms

Synonyms	Comment	Organism
ubiX	-	Colwellia psychrerythraea

Cofactor

Cofactor	Comment	Organism	Structure
FMN	-	Colwellia psychrerythraea

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Release 2023.1 (January 2023)