Family Report for: PhaC_cen_dom
| PhaC_cen_dom | Rank | 2 |
|---|
| Family | Abhydrolase_6 |
| Gene_locus (38) |
| Gene_locus_Frgt | 9bact-q4h1y5 |
| | 9prot-q7x588 |
| | 9psed-q4jhn4 |
| Block | X |
| Paper | Neoh_2022_Curr.Res.Biotechnol_4_87 |
| | Rehm_2003_Biochem.J_376_15 |
| | Kolibachuk_1999_Appl.Environ.Microbiol_65_3561 |
| Interpro | IPR010941 PhaC_cen_dom Poly-beta-hydroxybutyrate polymerase, central domain |
| 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 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. 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 |
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