Cloned (Comment) | Organism |
---|---|
gene SQD1, recombinant expression in Escherichia coli | Arabidopsis thaliana |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the affinity for sulfite of the native enzyme is at least 4fold higher compared to the recombinant spinach SQD1, whereas that for UDP-glucose is similar | Spinacia oleracea |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | SQD1 is a plastid UDP-glucose pyrophosphorylase | Chlamydomonas reinhardtii | 9507 | - |
chloroplast stroma | SQD1 is a soluble plastid UDP-glucose pyrophosphorylase | Spinacia oleracea | 9570 | - |
chloroplast stroma | SQDG1 is a soluble plastid UDP-glucose pyrophosphorylase | Arabidopsis thaliana | 9570 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
250000 | - |
- |
Spinacia oleracea |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-glucose + sulfite | Chlamydomonas reinhardtii | - |
UDP-alpha-D-sulfoquinovopyranose + H2O | - |
? | |
UDP-alpha-D-glucose + sulfite | Cereibacter sphaeroides | - |
UDP-alpha-D-sulfoquinovopyranose + H2O | - |
? | |
UDP-alpha-D-glucose + sulfite | Spinacia oleracea | - |
UDP-alpha-D-sulfoquinovopyranose + H2O | - |
? | |
UDP-alpha-D-glucose + sulfite | Arabidopsis thaliana | - |
UDP-alpha-D-sulfoquinovopyranose + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | - |
gene SQD1 | - |
Cereibacter sphaeroides | - |
gene sqdB | - |
Chlamydomonas reinhardtii | - |
gene SQD1 | - |
Spinacia oleracea | - |
gene SQD1 | - |
Purification (Comment) | Organism |
---|---|
native enzyme from the chloroplast stroma. Ferredoxin-dependent glutamate synthase, FdGOGAT, co-purifies and is tightly associated with SQD1 | Spinacia oleracea |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-glucose + sulfite | - |
Chlamydomonas reinhardtii | UDP-alpha-D-sulfoquinovopyranose + H2O | - |
? | |
UDP-alpha-D-glucose + sulfite | - |
Cereibacter sphaeroides | UDP-alpha-D-sulfoquinovopyranose + H2O | - |
? | |
UDP-alpha-D-glucose + sulfite | - |
Spinacia oleracea | UDP-alpha-D-sulfoquinovopyranose + H2O | - |
? | |
UDP-alpha-D-glucose + sulfite | - |
Arabidopsis thaliana | UDP-alpha-D-sulfoquinovopyranose + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
SQD1 | - |
Cereibacter sphaeroides |
SQD1 | - |
Chlamydomonas reinhardtii |
SQD1 | - |
Spinacia oleracea |
SQD1 | - |
Arabidopsis thaliana |
SqdB | - |
Cereibacter sphaeroides |
UDP-sulfoquinovose synthase | - |
Cereibacter sphaeroides |
UDP-sulfoquinovose synthase | - |
Arabidopsis thaliana |
General Information | Comment | Organism |
---|---|---|
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 | Chlamydomonas reinhardtii |
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 | Cereibacter sphaeroides |
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 | Spinacia oleracea |
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 | Arabidopsis thaliana |
additional information | 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 | Spinacia oleracea |
additional information | 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 | Arabidopsis thaliana |
physiological function | UDP-sulfoquinovose synthase, SqdB, is crucial for sulfolipid synthesis in the purple bacterium | Cereibacter sphaeroides |