protein THEM6 isoform 2 [Homo sapiens]
Protein Classification
thioesterase family protein( domain architecture ID 10594194)
thioesterase family protein belonging to the Hotdog fold superfamily, similar to 1,4-dihydroxy-2-naphthoyl-CoA hydrolase, which catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) during the synthesis of menaquinones and phylloquinone (vitamin K1)
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| 4HBT_2 | pfam13279 | Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
54-120 | 8.45e-15 | ||
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: 66.21 E-value: 8.45e-15
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| Name | Accession | Description | Interval | E-value | ||
| 4HBT_2 | pfam13279 | Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
54-120 | 8.45e-15 | ||
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: 66.21 E-value: 8.45e-15
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| 4HBT | cd00586 | 4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
49-120 | 6.38e-13 | ||
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: 61.08 E-value: 6.38e-13
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| FadM | COG0824 | Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ... |
49-120 | 1.96e-10 | ||
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: 55.29 E-value: 1.96e-10
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| Name | Accession | Description | Interval | E-value | ||
| 4HBT_2 | pfam13279 | Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
54-120 | 8.45e-15 | ||
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: 66.21 E-value: 8.45e-15
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| 4HBT | cd00586 | 4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
49-120 | 6.38e-13 | ||
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: 61.08 E-value: 6.38e-13
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| FadM | COG0824 | Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ... |
49-120 | 1.96e-10 | ||
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: 55.29 E-value: 1.96e-10
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| FatA | COG3884 | Acyl-ACP thioesterase [Lipid transport and metabolism]; |
53-72 | 3.19e-03 | ||
Acyl-ACP thioesterase [Lipid transport and metabolism]; Pssm-ID: 443092 [Multi-domain] Cd Length: 242 Bit Score: 36.47 E-value: 3.19e-03
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| hot_dog | cd03440 | The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
49-120 | 7.54e-03 | ||
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: 33.99 E-value: 7.54e-03
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