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C-terminal regulatory domain of Threonine dehydratase
Threonine dehydratases Pfam:PF00291 all contain a carboxy terminal region. This region may have a regulatory role. Some members contain two copies of this region. This family is homologous to the Pfam:PF01842 domain. [1]. 9562556. Structure and control of pyridoxal phosphate dependent. allosteric threonine deaminase.. Gallagher DT, Gilliland GL, Xiao G, Zondlo J, Fisher KE,. Chinchilla D, Eisenstein E;. Structure 1998;6:465-475. (from Pfam)
pyridoxal-phosphate dependent enzyme
Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16 Swiss:P04968, tryptophan synthase beta chain EC:4.2.1.20 Swiss:P00932, threonine synthase EC:4.2.99.2 Swiss:P04990, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22 Swiss:P35520, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4 Swiss:P76316. (from Pfam)
threonine ammonia-lyase IlvA
Catalyzes the formation of 2-oxobutanoate from L-threonine; biosynthetic
threonine ammonia-lyase, biosynthetic
This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (Pfam:PF00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain.
threonine ammonia-lyase
PLP-dependent threonine ammonia-lyase catalyzes the first deamination step in the degradation of threonine
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