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Family Report for: PHA_synth_I

PHA_synth_I



Relationship
Block X
Parent Family : Abhydrolase_6

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)

Database
Sequences
Interpro
|
IPR010941 (PhaC_cen_dom Poly-beta-hydroxybutyrate polymerase, central domain), IPR010963 (Poly(R)-hydroxyalkanoic acid synthase, class I)
PIRSF
|
Pdoc
|
PFam
|
PF07167 (PhaC_N)
Prints
|
Prosite
|
no EC number



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

References
2 more
    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: Cloning, molecular analysis, and expression of the polyhydroxyalkanoic acid synthase (phaC) gene from Chromobacterium violaceum
    Kolibachuk D, Miller A, Dennis D
    Ref: Applied Environmental Microbiology, 65:3561, 1999 : PubMed

            

Other Papers


No structure scheme yet for this family

Structures in PHA_synth_I family (4)

Genes Proteins in PHA_synth_I family (92)

Fragments of genes in PHA_synth_I family (1)

Substrates of some enzymes in the PHA_synth_I family (3)

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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