CATH Classification
Level | CATH Code | Description |
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3 | Alpha Beta |
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3.90 | Alpha-Beta Complex |
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3.90.1560 | putative 2-phosphosulfolactate phosphatase |
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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.
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UniProtKB Entries (1)
Q97E82 |
COMB_CLOAB
Clostridium acetobutylicum ATCC 824
Probable 2-phosphosulfolactate phosphatase
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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.
Proteins
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