poly(R)-hydroxyalkanoic acid synthase, partial [Halobacterium jilantaiense]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PhaC super family | cl43819 | Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; |
2-100 | 8.02e-44 | |||
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; The actual alignment was detected with superfamily member COG3243: Pssm-ID: 442475 [Multi-domain] Cd Length: 545 Bit Score: 148.56 E-value: 8.02e-44
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Name | Accession | Description | Interval | E-value | |||
PhaC | COG3243 | Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; |
2-100 | 8.02e-44 | |||
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; Pssm-ID: 442475 [Multi-domain] Cd Length: 545 Bit Score: 148.56 E-value: 8.02e-44
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PHA_synth_III_C | TIGR01836 | poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC ... |
2-99 | 2.52e-36 | |||
poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC subunit of a heterodimeric form of polyhydroxyalkanoic acid (PHA) synthase. Excepting the PhaC of Bacillus megaterium (which needs PhaR), all members require PhaE (TIGR01834) for activity and are designated class III. 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 polymerize short-chain-length hydroxyalkanoates. [Fatty acid and phospholipid metabolism, Biosynthesis] Pssm-ID: 130895 Cd Length: 350 Bit Score: 125.62 E-value: 2.52e-36
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PhaC_N | pfam07167 | Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal ... |
3-57 | 2.62e-06 | |||
Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal region 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 sulfur, becomes limiting. PHAs composed of monomeric units ranging from 3 to 14 carbons exist in nature. When the carbon source is exhausted, PHA is utilized by the bacterium. PhaC links D-(-)-3-hydroxybutyrl-CoA to an existing PHA molecule by the formation of an ester bond. This family appears to be a partial segment of an alpha/beta hydrolase domain. Pssm-ID: 462110 [Multi-domain] Cd Length: 173 Bit Score: 43.40 E-value: 2.62e-06
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Name | Accession | Description | Interval | E-value | |||
PhaC | COG3243 | Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; |
2-100 | 8.02e-44 | |||
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism]; Pssm-ID: 442475 [Multi-domain] Cd Length: 545 Bit Score: 148.56 E-value: 8.02e-44
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PHA_synth_III_C | TIGR01836 | poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC ... |
2-99 | 2.52e-36 | |||
poly(R)-hydroxyalkanoic acid synthase, class III, PhaC subunit; This model represents the PhaC subunit of a heterodimeric form of polyhydroxyalkanoic acid (PHA) synthase. Excepting the PhaC of Bacillus megaterium (which needs PhaR), all members require PhaE (TIGR01834) for activity and are designated class III. 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 polymerize short-chain-length hydroxyalkanoates. [Fatty acid and phospholipid metabolism, Biosynthesis] Pssm-ID: 130895 Cd Length: 350 Bit Score: 125.62 E-value: 2.52e-36
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PhaC_N | pfam07167 | Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal ... |
3-57 | 2.62e-06 | |||
Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal region 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 sulfur, becomes limiting. PHAs composed of monomeric units ranging from 3 to 14 carbons exist in nature. When the carbon source is exhausted, PHA is utilized by the bacterium. PhaC links D-(-)-3-hydroxybutyrl-CoA to an existing PHA molecule by the formation of an ester bond. This family appears to be a partial segment of an alpha/beta hydrolase domain. Pssm-ID: 462110 [Multi-domain] Cd Length: 173 Bit Score: 43.40 E-value: 2.62e-06
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Blast search parameters | ||||
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