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hotdog fold thioesterase [Cytobacillus gottheilii]
hotdog fold thioesterase( domain architecture ID 10794535)
hotdog fold thioesterase similar to Bacillus subtilis putative esterase ComA2 and to thioesterase PaaI that functions in the aerobic phenylacetate degradation pathway
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
unchar_dom_1 | TIGR00369 | uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ... |
7-124 | 1.07e-38 | |||
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown. : Pssm-ID: 161843 [Multi-domain] Cd Length: 117 Bit Score: 126.31 E-value: 1.07e-38
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Name | Accession | Description | Interval | E-value | |||
unchar_dom_1 | TIGR00369 | uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ... |
7-124 | 1.07e-38 | |||
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown. Pssm-ID: 161843 [Multi-domain] Cd Length: 117 Bit Score: 126.31 E-value: 1.07e-38
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PaaI | COG2050 | Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ... |
5-128 | 1.59e-38 | |||
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 441653 [Multi-domain] Cd Length: 138 Bit Score: 126.60 E-value: 1.59e-38
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PaaI_thioesterase | cd03443 | PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ... |
12-124 | 1.44e-34 | |||
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: 115.73 E-value: 1.44e-34
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PRK10254 | PRK10254 | proofreading thioesterase EntH; |
6-125 | 6.05e-32 | |||
proofreading thioesterase EntH; Pssm-ID: 182337 Cd Length: 137 Bit Score: 109.69 E-value: 6.05e-32
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4HBT | pfam03061 | Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
38-116 | 4.95e-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: 4.95e-17
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Name | Accession | Description | Interval | E-value | |||
unchar_dom_1 | TIGR00369 | uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ... |
7-124 | 1.07e-38 | |||
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown. Pssm-ID: 161843 [Multi-domain] Cd Length: 117 Bit Score: 126.31 E-value: 1.07e-38
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PaaI | COG2050 | Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ... |
5-128 | 1.59e-38 | |||
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 441653 [Multi-domain] Cd Length: 138 Bit Score: 126.60 E-value: 1.59e-38
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PaaI_thioesterase | cd03443 | PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ... |
12-124 | 1.44e-34 | |||
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: 115.73 E-value: 1.44e-34
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PRK10254 | PRK10254 | proofreading thioesterase EntH; |
6-125 | 6.05e-32 | |||
proofreading thioesterase EntH; Pssm-ID: 182337 Cd Length: 137 Bit Score: 109.69 E-value: 6.05e-32
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PRK10293 | PRK10293 | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase; |
26-125 | 1.58e-28 | |||
1,4-dihydroxy-2-naphthoyl-CoA hydrolase; Pssm-ID: 182360 Cd Length: 136 Bit Score: 101.24 E-value: 1.58e-28
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4HBT | pfam03061 | Thioesterase superfamily; This family contains a wide variety of enzymes, principally ... |
38-116 | 4.95e-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: 4.95e-17
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PLN02322 | PLN02322 | acyl-CoA thioesterase |
9-122 | 3.99e-15 | |||
acyl-CoA thioesterase Pssm-ID: 177956 Cd Length: 154 Bit Score: 67.40 E-value: 3.99e-15
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hot_dog | cd03440 | The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
24-123 | 7.25e-12 | |||
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: 57.49 E-value: 7.25e-12
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PaaD | TIGR02286 | phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ... |
9-125 | 3.62e-10 | |||
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway. Pssm-ID: 131339 Cd Length: 114 Bit Score: 53.19 E-value: 3.62e-10
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DUF4442 | pfam14539 | Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ... |
11-56 | 9.78e-04 | |||
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important. Pssm-ID: 434027 Cd Length: 131 Bit Score: 36.47 E-value: 9.78e-04
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Blast search parameters | ||||
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