Literature summary for 4.1.1.65 extracted from

Di Bartolomeo, F.; Doan, K.N.; Athenstaedt, K.; Becker, T.; Daum, G.
Involvement of a putative substrate binding site in the biogenesis and assembly of phosphatidylserine decarboxylase 1 from Saccharomyces cerevisiae (2017), Biochim. Biophys. Acta, 1862, 716-725 .

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Protein Variants

Protein Variants	Comment	Organism
G482P	mutation in conserved glycin residue, no major growth defect. The autocatalytic processing of G482P imported into mitochondria is delayed	Saccharomyces cerevisiae
G488P	mutation in conserved glycin residue, causes a dramatic growth defect of the mutant similar to that observed for a gene deletion mutant	Saccharomyces cerevisiae
G492P	mutation in conserved glycin residue, no major growth defect	Saccharomyces cerevisiae
K486A	mutation of the the most conserved Lys486 residue	Saccharomyces cerevisiae
additional information	removal of three to six amino acids of the conserved motif of the alpha subunit compromises the function of Psd1 as reflected by impaired growth of the mutants. In mutant Ax3, substitution of all positively charged amino acids of the highly conserved motif of the alpha subunit by alanine, the autocatalytic processing after import into mitochondria is delayed	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	the 56 kDa precursor is processed upon import into mitochondria, leading to a 4 kDa alpha-subunit and a 47 kDa beta-subunit. Mutations in the conserved motif of the alpha-subunit affect processing and stability of Psd1, and consequently the enzyme's activity	Saccharomyces cerevisiae	5739	-

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P39006	-	-

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Release 2023.1 (January 2023)