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beta-eliminating lyase-related protein
aminotransferase class V-fold PLP-dependent enzyme
This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-. (from Pfam)
aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
PLP-dependent transferase
This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor. [1]. 8831789. Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A. Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A;. J Mol Biol 1996;262:202-224. [2]. 9843488. Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution. Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A;. EMBO J 1998;17:6827-6838. (from Pfam)
DegT/DnrJ/EryC1/StrS family aminotransferase
The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA Swiss:P72454, StsC Swiss:P77952 and StsS [1]. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyses the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin [1]. [1]. 9238101. Identification of stsC, the gene encoding the L-glutamine:scyllo-inosose aminotransferase from streptomycin-producing Streptomycetes. Ahlert J, Distler J, Mansouri K, Piepersberg W;. Arch Microbiol 1997;168:102-113. (from Pfam)
selenocysteine lyase SclA
In bacteria, selenocysteine lyase activity (EC 4.4.1.16) usually is seen as a secondary activity of a cysteine desulfurase (EC 2.8.1.7). However, SclA, as studied in Enterococcus faecalis, acts primary on selenocysteine, binding cysteine just as well but acting on cysteine with much lower catalytic efficiency.
cysteine desulfurase family protein
This HMM describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family. Related families contain members active as cysteine desulfurases, selenocysteine lyases, or both. The members of this family form a distinct clade and all are shorter at the N-terminus. The function of this subfamily is unknown.
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