1 keywords

CATH Domain 1vr0C00

CATH Classification

Level CATH Code Description
Class 3 Alpha Beta
Architecture 3.90 Alpha-Beta Complex
Topology 3.90.1560 putative 2-phosphosulfolactate phosphatase
Homologous Superfamily 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
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