MULTISPECIES: tol-pal system-associated acyl-CoA thioesterase [Vibrio]
tol-pal system-associated acyl-CoA thioesterase( domain architecture ID 10798632)
tol-pal system-associated acyl-CoA thioesterase YbgC catalyzes the hydrolysis of short chain aliphatic acyl-CoA thioesters
List of domain hits
Name | Accession | Description | Interval | E-value | |||
thio_ybgC | TIGR02799 | tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical ... |
4-126 | 1.49e-68 | |||
tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical genes. Inner membrane proteins TolQ and TolR convert protomotive force to energy that is transduced through TolA to an outer membrane complex of TolB and Pal. The system is known to be required to maintain outer membrane integrity. In a system with several homologous parts, ExbB and ExbD transduces energy through TonB to a variety of outer membrane proteins, many of which are siderophore receptors. The tol-pal system therefore may also be involved in transport. This family consists of a protein nearly always found in operons with the genes of the tol-pal system. The significance of this thioesterase to the tol-pal system is unclear, but either of two observations may be relevant. First, Pal, or peptidoglycan-associated lipoprotein, has a conserved N-terminal cleavage and acylation that makes it a lipoprotein. Second, the tol-pal system is implicated not only in the import of certain organics but also in the maintenance of outer membrane integrity (by an unknown mechanism). : Pssm-ID: 274304 Cd Length: 126 Bit Score: 202.44 E-value: 1.49e-68
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Name | Accession | Description | Interval | E-value | |||
thio_ybgC | TIGR02799 | tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical ... |
4-126 | 1.49e-68 | |||
tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical genes. Inner membrane proteins TolQ and TolR convert protomotive force to energy that is transduced through TolA to an outer membrane complex of TolB and Pal. The system is known to be required to maintain outer membrane integrity. In a system with several homologous parts, ExbB and ExbD transduces energy through TonB to a variety of outer membrane proteins, many of which are siderophore receptors. The tol-pal system therefore may also be involved in transport. This family consists of a protein nearly always found in operons with the genes of the tol-pal system. The significance of this thioesterase to the tol-pal system is unclear, but either of two observations may be relevant. First, Pal, or peptidoglycan-associated lipoprotein, has a conserved N-terminal cleavage and acylation that makes it a lipoprotein. Second, the tol-pal system is implicated not only in the import of certain organics but also in the maintenance of outer membrane integrity (by an unknown mechanism). Pssm-ID: 274304 Cd Length: 126 Bit Score: 202.44 E-value: 1.49e-68
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PRK10800 | PRK10800 | acyl-CoA thioesterase YbgC; Provisional |
3-129 | 2.96e-58 | |||
acyl-CoA thioesterase YbgC; Provisional Pssm-ID: 182742 Cd Length: 130 Bit Score: 176.47 E-value: 2.96e-58
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FadM | COG0824 | Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ... |
3-127 | 1.58e-48 | |||
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis Pssm-ID: 440586 [Multi-domain] Cd Length: 139 Bit Score: 152.36 E-value: 1.58e-48
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4HBT | cd00586 | 4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
4-113 | 2.81e-40 | |||
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII). Pssm-ID: 238329 [Multi-domain] Cd Length: 110 Bit Score: 130.42 E-value: 2.81e-40
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4HBT_2 | pfam13279 | Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
13-126 | 7.12e-24 | |||
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily. Pssm-ID: 463826 Cd Length: 121 Bit Score: 88.94 E-value: 7.12e-24
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Name | Accession | Description | Interval | E-value | |||
thio_ybgC | TIGR02799 | tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical ... |
4-126 | 1.49e-68 | |||
tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical genes. Inner membrane proteins TolQ and TolR convert protomotive force to energy that is transduced through TolA to an outer membrane complex of TolB and Pal. The system is known to be required to maintain outer membrane integrity. In a system with several homologous parts, ExbB and ExbD transduces energy through TonB to a variety of outer membrane proteins, many of which are siderophore receptors. The tol-pal system therefore may also be involved in transport. This family consists of a protein nearly always found in operons with the genes of the tol-pal system. The significance of this thioesterase to the tol-pal system is unclear, but either of two observations may be relevant. First, Pal, or peptidoglycan-associated lipoprotein, has a conserved N-terminal cleavage and acylation that makes it a lipoprotein. Second, the tol-pal system is implicated not only in the import of certain organics but also in the maintenance of outer membrane integrity (by an unknown mechanism). Pssm-ID: 274304 Cd Length: 126 Bit Score: 202.44 E-value: 1.49e-68
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PRK10800 | PRK10800 | acyl-CoA thioesterase YbgC; Provisional |
3-129 | 2.96e-58 | |||
acyl-CoA thioesterase YbgC; Provisional Pssm-ID: 182742 Cd Length: 130 Bit Score: 176.47 E-value: 2.96e-58
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FadM | COG0824 | Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ... |
3-127 | 1.58e-48 | |||
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis Pssm-ID: 440586 [Multi-domain] Cd Length: 139 Bit Score: 152.36 E-value: 1.58e-48
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TIGR00051 | TIGR00051 | acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ... |
7-123 | 7.89e-45 | |||
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General] Pssm-ID: 129161 [Multi-domain] Cd Length: 117 Bit Score: 142.17 E-value: 7.89e-45
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4HBT | cd00586 | 4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
4-113 | 2.81e-40 | |||
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII). Pssm-ID: 238329 [Multi-domain] Cd Length: 110 Bit Score: 130.42 E-value: 2.81e-40
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4HBT_2 | pfam13279 | Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
13-126 | 7.12e-24 | |||
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily. Pssm-ID: 463826 Cd Length: 121 Bit Score: 88.94 E-value: 7.12e-24
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4HBT | pfam03061 | Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
18-103 | 5.59e-17 | |||
Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters. Pssm-ID: 427116 [Multi-domain] Cd Length: 79 Bit Score: 69.98 E-value: 5.59e-17
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hot_dog | cd03440 | The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
7-110 | 1.01e-14 | |||
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis. Pssm-ID: 239524 [Multi-domain] Cd Length: 100 Bit Score: 64.80 E-value: 1.01e-14
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Blast search parameters | ||||
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