Literature summary for 3.6.1.13 extracted from

Karuppiah, V.; Thistlethwaite, A.; Dajani, R.; Warwicker, J.; Derrick, J.P.
Structure and mechanism of the bifunctional CinA enzyme from Thermus thermophilus (2014), J. Biol. Chem., 289, 33187-33197.

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.16 A resolution. The crystal structure shows an unusual asymmetric dimer, with three domains for each chain. The C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose diphosphatase activity. The mechanism for the ADP-ribose diphosphatase reaction involves a rotation of the COG1058 domain dimer as part of the reaction cycle	Thermus thermophilus

Crystallization (Comment)

Organism

to 2.16 A resolution. The crystal structure shows an unusual asymmetric dimer, with three domains for each chain. The C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose diphosphatase activity. The mechanism for the ADP-ribose diphosphatase reaction involves a rotation of the COG1058 domain dimer as part of the reaction cycle

Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	Q5SHB0	enzyme displays both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities	-
Thermus thermophilus DSM 579	Q5SHB0	enzyme displays both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities	-

Synonyms

Synonyms	Comment	Organism
CinA	-	Thermus thermophilus

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Release 2023.1 (January 2023)