PhaC_cen_dom

Relationship

Family: PhaC_cen_dom

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 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)

Database

Interpro : IPR010941 PhaC_cen_dom Poly-beta-hydroxybutyrate polymerase, central domain

PIRSF : No PIRSF

Pdoc : No Pdoc

Pfam : PF07167 PhaC_N

Prints : No Print

EC Number : No EC Number

Sequences

Peptide in Fasta
Nucleotide in Fasta
Alignment with Multalin Text only
Seed alignment with MAFFT No colour
Alignment with MAFFT No colour
Dendrogram The dnd file

References (3)

Title : Polyhydroxyalkanoate synthase (PhaC): The key enzyme for biopolyester synthesis - Neoh_2022_Curr.Res.Biotechnol_4_87
Author(s) : Neoh SZ , Chek MF , Tan HT , Linares-Pasten JA , Nandakumar A , Hakoshima T , Sudesh K
Ref : Current Research in Biotechnology , 4 :87 , 2022
Abstract : Neoh_2022_Curr.Res.Biotechnol_4_87
ESTHER : Neoh_2022_Curr.Res.Biotechnol_4_87
PubMedSearch : Neoh_2022_Curr.Res.Biotechnol_4_87
PubMedID:

Title : Polyester synthases: natural catalysts for plastics - Rehm_2003_Biochem.J_376_15
Author(s) : Rehm BH
Ref : Biochemical Journal , 376 :15 , 2003
Abstract : Rehm_2003_Biochem.J_376_15
ESTHER : Rehm_2003_Biochem.J_376_15
PubMedSearch : Rehm_2003_Biochem.J_376_15
PubMedID: 12954080

Title : Cloning, molecular analysis, and expression of the polyhydroxyalkanoic acid synthase (phaC) gene from Chromobacterium violaceum - Kolibachuk_1999_Appl.Environ.Microbiol_65_3561
Author(s) : Kolibachuk D , Miller A , Dennis D
Ref : Applied Environmental Microbiology , 65 :3561 , 1999
Abstract : Kolibachuk_1999_Appl.Environ.Microbiol_65_3561
ESTHER : Kolibachuk_1999_Appl.Environ.Microbiol_65_3561
PubMedSearch : Kolibachuk_1999_Appl.Environ.Microbiol_65_3561
PubMedID: 10427049
Gene_locus related to this paper: chrvi-PHAC , vibpa-PHAC

No structure scheme yet for this family

Genes Proteins in PhaC_cen_dom family (35)

Fragments of genes in PhaC_cen_dom family (3)

No fragment of genes

No substrate

No Inhibitor