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Items: 8

1.

Threonine synthase N terminus

This domain is found at the N-terminus of many threonine synthase enzymes [1]. [1]. 11756443. Structure and function of threonine synthase from yeast. Garrido-Franco M, Ehlert S, Messerschmidt A, Marinkovic' S, Huber R, Laber B, Bourenkov GP, Clausen T;. J Biol Chem. 2002;277:12396-12405. (from Pfam)

Date:
2024-10-16
Family Accession:
NF026171.5
Method:
HMM
2.

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)

Date:
2024-08-14
Family Accession:
NF012512.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

threonine synthase

threonine synthase catalyzes the final step of threonine biosynthesis, the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine

Date:
2023-02-22
Family Accession:
10107520
Method:
Sparcle
8.

threonine synthase

Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model.

Gene:
thrC
GO Terms:
Molecular Function:
threonine synthase activity (GO:0004795)
Biological Process:
threonine biosynthetic process (GO:0009088)
Date:
2021-04-27
Family Accession:
TIGR00260.1
Method:
HMM
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