CATH Domain 2woqA00

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.20	Alpha-Beta Barrel
	3.20.20	TIM Barrel
	3.20.20.70	Aldolase class I

Domain Context

CATH Clusters

Superfamily	Aldolase class I
Functional Family	Delta-aminolevulinic acid dehydratase

Enzyme Information

4.2.1.24

Porphobilinogen synthase.

based on mapping to UniProt Q59643

2 5-aminolevulinate = porphobilinogen + 2 H(2)O.

-!- The enzyme catalyzes the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430. -!- The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis. -!- In humans, the enzyme is a primary target for the environmental toxin Pb. -!- The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation.

UniProtKB Entries (1)

Q59643

HEM2_PSEAE

Pseudomonas aeruginosa PAO1

Delta-aminolevulinic acid dehydratase

PDB Structure

PDB	2WOQ
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Structure of the heme biosynthetic Pseudomonas aeruginosa porphobilinogen synthase in complex with the antibiotic alaremycin. Heinemann, I.U., Schulz, C., Schubert, W.D., Heinz, D.W., Wang, Y.G., Kobayashi, Y., Awa, Y., Wachi, M., Jahn, D., Jahn, M. Antimicrob. Agents Chemother.