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Family Report for: PHA_synth_III_C


Block X
Parent Family : Abhydrolase_6

(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 PhaC subunit of a heterodimeric form of polyhydroxyalkanoic acid (PHA) synthase. Excepting the PhaC of Bacillus megaterium (which needs PhaR is not an a/b hydrolase), all members require PhaE (IPR010123 PhaE is not an a/b hydrolase) subunit for activity and are designated class III. (PhaC of Bacillus associated to PhaR are designed Class IV PHA_synth_IV but are not separated here) . This enzyme builds ester polymers for carbon and energy storage that accumulate in inclusions, and both this enzyme and the depolymerase associate with the inclusions. Class III enzymes polymerise short-chain-length hydroxyalkanoates. 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)

IPR010941 (PhaC_cen_dom Poly-beta-hydroxybutyrate polymerase, central domain), IPR010125 (Poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit PHA_synth_III_C)
PF07167 (PhaC_N)
no EC number

Peptide in
Nucleotide in
Alignment with Multalin
|Text only/graphic display
Seed alignment with MAFFT
|No colour/coloured with Mview
Alignment with MAFFT
|No colour/coloured with Mview
|Graphical display, obtained with the dnd file produced by Clustalw

    Title: Polyhydroxyalkanoate synthase (PhaC): The key enzyme for biopolyester synthesis
    Neoh SZ, Chek MF, Tan HT, Linares-Pasten JA, Nandakumar A, Hakoshima T, Sudesh K
    Ref: Current Research in Biotechnology, 4:87, 2022 : PubMed


    Title: Polyester synthases: natural catalysts for plastics
    Rehm BH
    Ref: Biochemical Journal, 376:15, 2003 : PubMed


    Title: PhaC and PhaR are required for polyhydroxyalkanoic acid synthase activity in Bacillus megaterium
    McCool GJ, Cannon MC
    Ref: Journal of Bacteriology, 183:4235, 2001 : PubMed


Other Papers

No structure scheme yet for this family

No Structure yet in this family

Genes Proteins in PHA_synth_III_C family (98)

No fragments
Substrates of some enzymes in the PHA_synth_III_C family (1)

No Inhibitor

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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