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phosphopantothenoylcysteine decarboxylase
The DNA/pantothenate metabolism flavoprotein (EC:4.1.1.36) affects synthesis of DNA, and pantothenate metabolism. [1]. 3123465. beta-Alanine auxotrophy associated with dfp, a locus affecting. DNA synthesis in Escherichia coli.. Spitzer ED, Jimenez-Billini HE, Weiss B;. J Bacteriol 1988;170:872-876. (from Pfam)
flavoprotein
This family contains diverse flavoprotein enzymes. This family includes epidermin biosynthesis protein, EpiD Swiss:P30197, which has been shown to be a flavoprotein that binds FMN [1]. This enzyme catalyses the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond. This family also includes the B chain of dipicolinate synthase a small polar molecule that accumulates to high concentrations in bacterial endospores, and is thought to play a role in spore heat resistance, or the maintenance of heat resistance [2]. dipicolinate synthase catalyses the formation of dipicolinic acid from dihydroxydipicolinic acid. This family also includes phenyl-acrylic acid decarboxylase Swiss:P33751 (EC:4.1.1.-) [3]. [1]. 1644762. Purification and characterization of EpiD, a flavoprotein. involved in the biosynthesis of the lantibiotic epidermin.. Kupke T, Stevanovic S, Sahl HG, Gotz F;. J Bacteriol 1992;174:5354-5361.. [2]. 8345520. Cloning, DNA sequence, functional analysis and transcriptional. regulation of the genes encoding dipicolinic acid synthetase. required for sporulation in Bacillus subtilis.. Daniel RA, Errington J;. J Mol Biol 1993;232:468-483.. [3]. 8181743. PAD1 encodes phenylacrylic acid decarboxylase which confers. resistance to cinnamic acid in Saccharomyces cerevisiae.. Clausen M, Lamb CJ, Megnet R, Doerner PW;. Gene 1994;142:107-112. (from Pfam)
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase
bifunctional phosphopantothenoylcysteine decarboxylase (CoaC)/phosphopantothenate synthase (CoaB) catalyzes two steps in the biosynthesis of coenzyme A, the conjugation of cysteine to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, followed by its decarboxylation to form 4'-phosphopantotheine
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase CoaBC
This HMM represents a bifunctional enzyme that catalyzes the second and third steps (cysteine ligation, EC 6.3.2.5, and decarboxylation, EC 4.1.1.36) in the biosynthesis of coenzyme A (CoA) from pantothenate in bacteria. In early descriptions of this flavoprotein, a ts mutation in one region of the protein appeared to cause a defect in DNA metaobolism rather than an increased need for the pantothenate precursor beta-alanine. This protein was then called dfp, for DNA/pantothenate metabolism flavoprotein. The authors responsible for detecting phosphopantothenate--cysteine ligase activity suggest renaming this bifunctional protein coaBC for its role in CoA biosynthesis. This enzyme contains the FMN cofactor, but no FAD or pyruvoyl group. The amino-terminal region contains the phosphopantothenoylcysteine decarboxylase activity.
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