EC Number   |
General Information |
Reference |
|---|
    3.13.1.1 | malfunction |
in-frame deletion of agl3 results in a decreased molecular mass of the S-layer glycoprotein SlaA and the flagellin FlaB, indicating a change in the N-glycan composition with reduced trisaccharide structure composed of Man1GlcNAc2, missing the sulfoquinovose, a mannose and glucose. Cells lacking agl3 had a significantly lower growth rate at elevated salt concentrations compared with the background strain, overview |
-, 720497 |
| 3.13.1.1 | metabolism |
key elements of the sulfite network enzymes that include adenosine-5'-phosphosulfate reductase and the sulfite scavengers sulfite oxidase (SO), sulfite reductase, UDP-sulfoquinovose synthase, and beta-mercaptopyruvate sulfurtransferases. During extended dark, sulfite oxidase is enhanced in Solanum lycopersicum wild-type leaves, while the other sulfite network components are downregulated. One pathway for sulfite utilization is its incorporation into sulfolipids, catalyzed by the chloroplast-localized UDP-sulfoquinovose synthase. In the first step, UDP-sulfoquinovase is catalyzed by SQD1, employing sulfite and UDP-Glc as substrates, while in the second step, sulfoquinovosyldiacylglycerol (SQDG) is catalyzed by SQDG synthase, employing UDP-sulfoquinovose and diacylglycerols as substrates |
726230 |
| 3.13.1.1 | metabolism |
the enzyme is critical for biosynthesis of UDP-sulfoquinovose |
-, 720497 |
| 3.13.1.1 | metabolism |
UDP-sulfoquinovose synthase, SQD1, is important in sulfoquinovosyldiacylglycerol, SQDG, biosynthesis together with the SQDG synthase, SQD2, mechanism for SQDG biosynthesis, overview. Sulfoquinovosyldiacylglycerol is the only sulfur-containing anionic glycerolipid, a relatively minor relatively minor, and is the least prevalent component of photosynthetic membrane lipids. The function of SQDG under phosphate-limited growth conditions is highly correlated with the regulation of other plant glycerolipid biosyntheses |
723680 |
| 3.13.1.1 | more |
ferredoxin-dependent glutamate synthase, FdGOGAT, co-purifies with the native SQD1 from chloroplast stroma and is tightly associated with the enzyme. FdGOGAT is a flavincontaining protein that can reversibly bind sulfite, suggesting that the protein efficiently delivers sulfite to the SQD1 active site |
723680 |
| 3.13.1.1 | more |
the enzyme forms a complex with ferredoxin-dependent glutamate synthase, FdGOGAT, tentative modeling of SQDG1 bound to FdGOGAT from Synechococcus sp. PCC 6803, the predicted SQD1 sulfite channel is directed at the FMN cofactor in the FdGOGAT FMN-binding domain. FdGOGAT interaction with SQD1 channels sulfite directly to SQD1 and is an efficient way to overcome this problem |
723680 |
| 3.13.1.1 | physiological function |
the enzyme is a member of the sulfite network, one pathway for sulfite utilization is its incorporation into sulfolipids, catalyzed by the chloroplast-localized UDP-sulfoquinovose synthase. The degradation of sulfolipids is an essential step in chloroplast degradation |
726230 |
| 3.13.1.1 | physiological function |
UDP-sulfoquinovose synthase, SqdB, is crucial for sulfolipid synthesis in the purple bacterium |
723680 |
