CATH Classification

Domain Context

CATH Clusters

Superfamily Hotdog Thioesterase
Functional Family 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ

Enzyme Information

4.2.1.59
3-hydroxyacyl-[acyl-carrier-protein] dehydratase.
based on mapping to UniProt Q2SWY7
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.

UniProtKB Entries (1)

Q2SWY7
FABZ_BURTA
Burkholderia thailandensis E264
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ

PDB Structure

PDB 4H4G
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Combining functional and structural genomics to sample the essential Burkholderia structome.
Baugh, L., Gallagher, L.A., Patrapuvich, R., Clifton, M.C., Gardberg, A.S., Edwards, T.E., Armour, B., Begley, D.W., Dieterich, S.H., Dranow, D.M., Abendroth, J., Fairman, J.W., Fox, D., Staker, B.L., Phan, I., Gillespie, A., Choi, R., Nakazawa-Hewitt, S., Nguyen, M.T., Napuli, A., Barrett, L., Buchko, G.W., Stacy, R., Myler, P.J., Stewart, L.J., Manoil, C., Van Voorhis, W.C.
Plos One