Protein Family Models

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)

Date:

2024-10-16

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)

Date:

2024-08-14

Catalyzes the formation of 2-oxobutanoate from L-threonine; biosynthetic

Gene:

ilvA

Date:

2021-08-05

This HMM represents threonine dehydratase, the first step in the pathway converting threonine into isoleucine. At least two other clades of biosynthetic threonine dehydratases have been charcterized by HMM models (TIGR01124 and TIGR01127). Those sequences described by this model are exclusively found in species containg the rest of the isoleucine pathway and which are generally lacking in members of the those other two clades of threonine dehydratases. Members of this clade are also often gene clustered with other elements of the isoleucine pathway.

Gene:

ilvA

Date:

2024-05-30

PLP-dependent threonine ammonia-lyase catalyzes the first deamination step in the degradation of threonine

Date:

2017-03-23