CATH Domain 2feaB01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.50	Rossmann fold
	3.40.50.1000	HAD superfamily/HAD-like

Domain Context

CATH Clusters

Superfamily	HAD superfamily/HAD-like
Functional Family

Enzyme Information

3.1.3.87

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase.

based on mapping to UniProt O31667

2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate + H(2)O = 1,2- dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.

-!- The enzyme participates in the methionine salvage pathway in Bacillus subtilis. -!- In some species a single bifunctional enzyme, EC 3.1.3.77, catalyzes both this reaction and that of EC 5.3.2.5. -!- Formerly EC 3.1.3.n4.

UniProtKB Entries (1)

O31667

MTNX_BACSU

Bacillus subtilis subsp. subtilis str. 168

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase

PDB Structure

PDB	2FEA
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 A resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate. Xu, Q., Saikatendu, K.S., Krishna, S.S., McMullan, D., Abdubek, P., Agarwalla, S., Ambing, E., Astakhova, T., Axelrod, H.L., Carlton, D., Chiu, H.J., Clayton, T., DiDonato, M., Duan, L., Elsliger, M.A., Feuerhelm, J., Grzechnik, S.K., Hale, J., Hampton, E., Han, G.W., Haugen, J., Jaroszewski, L., Jin, K.K., Klock, H.E., Knuth, M.W., Koesema, E., Miller, M.D., Morse, A.T., Nigoghossian, E., Okach, L., Oommachen, S., Paulsen, J., Reyes, R., Rife, C.L., Schwarzenbacher, R., van den Bedem, H., White, A., Wolf, G., Hodgson, K.O., Wooley, J., Deacon, A.M., Godzik, A., Lesley, S.A., Wilson, I.A. Proteins

Network disruptions