CATH Domain 1vr0A00

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.90	Alpha-Beta Complex
	3.90.1560	putative 2-phosphosulfolactate phosphatase
	3.90.1560.10	ComB-like

Domain Context

CATH Clusters

Superfamily	ComB-like
Functional Family	Probable 2-phosphosulfolactate phosphatase

Enzyme Information

3.1.3.71

2-phosphosulfolactate phosphatase.

based on mapping to UniProt Q97E82

(2R)-2-phospho-3-sulfolactate + H(2)O = (2R)-3-sulfolactate + phosphate.

-!- The enzyme from Methanococcus jannaschii acts on both stereoisoimers of the substrate and also hydrolyzes a number of phosphate monoesters of (S)-2-hydroxycarboxylic acids, including 2-phosphomalate, 2-phospholactate and 2-phosphoglycolate. -!- This enzyme can also hydrolyze phosphate monoesters of (R)-2- hydroxycarboxylic acids such as (S)-2-phospho-3-sulfolactate and (R)- 2-phosphomalate, which, presumably, bind to the enzyme in opposite orientations.

UniProtKB Entries (1)

Q97E82

COMB_CLOAB

Clostridium acetobutylicum ATCC 824

Probable 2-phosphosulfolactate phosphatase

PDB Structure

PDB	1VR0
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Crystal structure of 2-phosphosulfolactate phosphatase (ComB) from Clostridium acetobutylicum at 2.6 A resolution reveals a new fold with a novel active site. DiDonato, M., Krishna, S.S., Schwarzenbacher, R., McMullan, D., Agarwalla, S., Brittain, S.M., Miller, M.D., Abdubek, P., Ambing, E., Axelrod, H.L., Canaves, J.M., Chiu, H.J., Deacon, A.M., Duan, L., Elsliger, M.A., Godzik, A., Grzechnik, S.K., Hale, J., Hampton, E., Haugen, J., Jaroszewski, L., Jin, K.K., Klock, H.E., Knuth, M.W., Koesema, E., Kreusch, A., Kuhn, P., Lesley, S.A., Levin, I., Morse, A.T., Nigoghossian, E., Okach, L., Oommachen, S., Paulsen, J., Quijano, K., Reyes, R., Rife, C.L., Spraggon, G., Stevens, R.C., van den Bedem, H., White, A., Wolf, G., Xu, Q., Hodgson, K.O., Wooley, J., Wilson, I.A. Proteins