CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.10 | Roll | |
3.10.129 | Thiol Ester Dehydrase; Chain A | |
3.10.129.10 | Hotdog Thioesterase |
Domain Context
CATH Clusters
Superfamily | Hotdog Thioesterase |
Functional Family | 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase |
Enzyme Information
5.3.3.14 |
Trans-2-decenoyl-[acyl-carrier-protein] isomerase.
based on mapping to UniProt P0A6Q3
Trans-dec-2-enoyl-[acyl-carrier-protein] = cis-dec-3-enoyl-[acyl-carrier- protein].
-!- While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs. -!- ACP can be replaced by either CoA or N-acetylcysteamine thioesters. -!- The cis-3-enoyl product is required to form unsaturated fatty acids, such as palmitoleic acid and cis-vaccenic acid, in dissociated (or type II) fatty-acid biosynthesis.
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4.2.1.59 |
3-hydroxyacyl-[acyl-carrier-protein] dehydratase.
based on mapping to UniProt P0A6Q3
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl- carrier protein] + H(2)O.
-!- This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria. -!- The enzyme uses fatty acyl thioesters of ACP in vivo. -!- Different forms of the enzyme may have preferences for substrates with different chain length. -!- For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length. -!- Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyzes EC 5.3.3.14. -!- Despite the differences both forms can catalyze all steps leading to the synthesis of palmitate (C16:0). -!- FabZ, but not FabA, can also accept unsaturated substrates. -!- Formerly EC 4.2.1.58, EC 4.2.1.60 and EC 4.2.1.61.
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UniProtKB Entries (1)
P0A6Q3 |
FABA_ECOLI
Escherichia coli K-12
3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
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PDB Structure
PDB | 1MKA |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site.
Structure
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