Family Report for: PHA_synth_I
PHA_synth_I | Rank | 2 |
| Family | Abhydrolase_6 |
| Gene_locus (93) |
| Gene_locus_Frgt | pseol-PHBC |
| Block | X |
| Paper (5) |
| Structure | 5XAV |
| | 6K3C |
| | 5T6O |
| | 5HZ2 |
| Interpro | IPR010941 PhaC_cen_dom Poly-beta-hydroxybutyrate polymerase, central domain |
| | IPR010963 Poly(R)-hydroxyalkanoic acid synthase, class I |
| Comment | (The family Pha_synthase was split in four families (PHA_synth_I, PHA_synth_II, PHA_synth_III, PhaC_cen_dom ) according to Interpro and Tigrpfam. PhaC_cen_dom groups enzyme with the central domain but not the class I,II,III domains)This entry represents the class I subfamily of poly(R)-hydroxyalkanoate synthases, which polymerises hydroxyacyl-CoAs with three to five carbons in the hydroxyacyl backbone into aliphatic esters termed poly(R)-hydroxyalkanoic acids. These polymers accumulate as carbon and energy storage inclusions in many species and can amount to 90 percent of the dry weight of the cell. Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus. This entry represents the central domain of the bacterial poly-beta-hydroxybutyrate polymerase (PhaC). Polyhydroxyalkanoic acids (PHAs) are carbon and energy reserve polymers produced in some bacteria when carbon sources are plentiful and another nutrient, such as nitrogen, phosphate, oxygen, or sulphur, becomes limiting. PHAs composed of monomeric units ranging from 3 to 14 carbons exist in nature. When the carbon source is exhausted, PHA is utilised by the bacterium. PhaC links D-(-)-3-hydroxybutyrl-CoA to an existing PHA molecule by the formation of an ester bond PHA_synth_I TIGR01838 PHA_synth_II TIGR01839. The nucleophilic residue of the catalytic triad is a cysteine (with exceptions) |
| Pfam | PF07167 PhaC_N |
| News | DECEMBER-07-2016 |
| Substrate | P(3HB-co-4HB) |
| | P(3HB-co-3HHx) |
| | 3HB-CoA |
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