unnamed protein product [Oryza sativa Japonica Group]
hotdog family protein( domain architecture ID 107)
hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate
List of domain hits
Name | Accession | Description | Interval | E-value | |||
hot_dog super family | cl00509 | The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
43-153 | 1.20e-07 | |||
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. The actual alignment was detected with superfamily member cd03443: Pssm-ID: 469797 [Multi-domain] Cd Length: 113 Bit Score: 47.55 E-value: 1.20e-07
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Name | Accession | Description | Interval | E-value | |||
PaaI_thioesterase | cd03443 | PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ... |
43-153 | 1.20e-07 | |||
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ). Pssm-ID: 239527 [Multi-domain] Cd Length: 113 Bit Score: 47.55 E-value: 1.20e-07
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PaaI | COG2050 | Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ... |
35-150 | 6.75e-06 | |||
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 441653 [Multi-domain] Cd Length: 138 Bit Score: 43.39 E-value: 6.75e-06
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4HBT | pfam03061 | Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
99-146 | 5.03e-05 | |||
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: 39.93 E-value: 5.03e-05
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Name | Accession | Description | Interval | E-value | |||
PaaI_thioesterase | cd03443 | PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ... |
43-153 | 1.20e-07 | |||
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ). Pssm-ID: 239527 [Multi-domain] Cd Length: 113 Bit Score: 47.55 E-value: 1.20e-07
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PaaI | COG2050 | Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ... |
35-150 | 6.75e-06 | |||
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 441653 [Multi-domain] Cd Length: 138 Bit Score: 43.39 E-value: 6.75e-06
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4HBT | pfam03061 | Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
99-146 | 5.03e-05 | |||
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: 39.93 E-value: 5.03e-05
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FadM | COG0824 | Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ... |
91-151 | 5.23e-05 | |||
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: 41.04 E-value: 5.23e-05
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hot_dog | cd03440 | The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
56-153 | 9.27e-05 | |||
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: 39.77 E-value: 9.27e-05
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4HBT | cd00586 | 4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
91-151 | 1.80e-03 | |||
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: 36.04 E-value: 1.80e-03
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Blast search parameters | ||||
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