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Links from Protein

Items: 5

1.

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme

GO Terms:
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
pyridoxal phosphate binding (GO:0030170)
Date:
2024-08-14
Family Accession:
NF012382.5
Method:
HMM
2.
new record, indexing in progress
Family Accession:
3.
new record, indexing in progress
Family Accession:
4.

PatB family C-S lyase

Characterized members of this subfamily are known or probable C-S lyases from a family of pyridoxal phosphate-dependent enzymes that tend to be (mis)annotated as probable aminotransferases. One member is PatB of Bacillus subtilis, a proven C-S-lyase. Another is the virulence factor cystalysin from Treponema denticola, whose hemolysin activity may stem from H2S production. Members of the seed alignment occur next to examples of the enzyme 5-histidylcysteine sulfoxide synthase, from ovothiol A biosynthesis, and would be expected to perform a C-S cleavage of 5-histidylcysteine sulfoxide to leave 1-methyl-4-mercaptohistidine (ovothiol A). The PatB from Staphylococcus hominis (ShPatB) is a C-S lyase active on aliphatic cysteine-S-conjugates; its release of the thioalcohol 3-methyl-3-sulfanylhexan-1-ol (3M3SH) from the odourless precursor Cys-Gly-3M3SH secreted from human skin is a major contributor to body odor.

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
pyridoxal phosphate binding (GO:0030170)
Date:
2021-08-12
Family Accession:
TIGR04350.1
Method:
HMM
5.

MalY/PatB family protein

MalY/PatB family protein acts as a beta-cystathionase, catalyzing the transformation of cystathionine to homocysteine, similar to Escherichia coli MalY and Bacillus subtilis PatB; belongs to the pyridoxal phosphate (PLP)-dependent aminotransferase superfamily

Date:
2024-08-07
Family Accession:
11439426
Method:
Sparcle
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