EC Number   |
General Information |
Reference |
|---|
    2.7.8.7 | evolution |
BPSS2266 is a PPTase of the 4'-phosphopantetheinyl transferase superfamily |
-, 739157 |
| 2.7.8.7 | evolution |
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases |
-, 739157 |
| 2.7.8.7 | evolution |
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. Pseudomonas aeruginosa contains one Sfp-type PPTase, PaPcpS or PcpS with broad substrate specificity, but no AcpS-type PPTase |
-, 739157 |
| 2.7.8.7 | evolution |
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain |
-, 739157 |
| 2.7.8.7 | evolution |
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain. The toxin found in a hybrid PKS-NRPS cluster, (also known as PKS island) produces colibactin. Within this cluster, clbA is identified as a PPTase |
739157 |
| 2.7.8.7 | evolution |
phylogenetic analyses of plant PPT/PPT-like homologues, overview |
739319 |
| 2.7.8.7 | evolution |
PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively |
-, 739683 |
| 2.7.8.7 | evolution |
SchPPT is a group II PPTase |
-, 737568 |
| 2.7.8.7 | malfunction |
a conditional pptT mutant in Mycobacterium. tuberculosis H37Rv shows retarded growth and persistence. Mutant cells fail to multiply in vivo |
-, 739157 |
| 2.7.8.7 | malfunction |
a T-DNA-tagged null mutant mtppt-1 allele shows an embryo-lethal phenotype. Arabidopsis thaliana RNAi transgenic lines with reduced mtPPT expression display typical phenotypes associated with a deficiency in the mtFAS system, namely miniaturized plant morphology, slow growth, reduced lipoylation of mitochondrial proteins, and the hyperaccumulation of photorespiratory intermediates, glycine and glycolate. the seeds in the mtppt-1 mutant plants failed to develop normally. These morphological and metabolic alterations are reversed when these plants are grown in a non-photorespiratory condition (i.e. 1% CO2 atmosphere), because they are a consequence of a deficiency in photorespiration due to the reduced lipoylation of the photorespiratory glycine decarboxylase. Phenotypes, detailed overview |
739319 |
