Any feedback?
Information on EC 3.13.1.1 - UDP-sulfoquinovose synthase
for references in articles please use BRENDA:EC3.13.1.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.13.1.1 UDP-sulfoquinovose synthaseIUBMB Comments
Requires NAD+, which appears to oxidize UDP-alpha-D-glucose to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite is added. The reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite.
Specify your search results
Word Map
- 3.13.1.1
- sulfolipid
- sulfoquinovosyldiacylglycerols
- thylakoid
-
sulfoquinovosyl
- phosphatidylglycerol
- elongatus
- environmental protection
- acidocaldarius
-
photosystem
-
exohydrolase
- monogalactosyldiacylglycerols
-
loosening
-
perennial
- energy production
-
bentgrass
- glucan
-
creeping
- stolonifera
-
penncross
-
irrigated
-
sulfur-containing
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
udp-sulfoquinovose synthase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Agl3
Desulfinase
DszB
SQD1
sulfite:UDP-glucose sulfotransferase
synthase, uridine diphosphosulfoquinovose
-
-
-
-
UDP-sulfoquinovose synthase
sulfite:UDP-glucose sulfotransferase
-
-
-
-
UDP-sulfoquinovose synthase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
a decrease in the internal phosphate concentration shows a corresponding increase in the relative amount of sulfolipid with UDP-sulfoquinovose as precursor
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
contains characteristic conserved Y-XXX-K and glycine-rich sequence patterns
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
sequence similarity to sugar nucleotide modifying enzymes, Thr228 seems to be catalytically important
-
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
short-chain dehydrogenase/reductase family
-
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
short-chain dehydrogenase/reductase family
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
requires NAD+, which appears to oxidize the substrate to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sufite can add. The reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite
-
-
-
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
required NAD+ appears to oxidize the substrate to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite can add, the reaction is completed when the substrate is rehydrogenated at C-4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-S bond
-
-
-
-
hydrolysis of sulfonic acid
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
UDP-6-sulfo-6-deoxyglucose sulfohydrolase
Requires NAD+, which appears to oxidize UDP-alpha-D-glucose to UDP-4-dehydroglucose, which dehydrates to UDP-4-dehydro-6-deoxygluc-5-enose, to which sulfite is added. The reaction is completed when the substrate is rehydrogenated at C-4. The enzyme from Arabidopsis thaliana is specific for UDP-Glc and sulfite.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
337378-74-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-sulfoquinovopyranose + H2O
UDP-alpha-D-glucose + sulfite
the enzyme catalyzes the reverse reaction
-
-
?
UDP-glucose + ?
UDP-sulfoquinovose + H2O
-
first step of sulfolipid biosynthesis, unknown sulfur donor
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
the microbial conversion of DBT into 2-HBP is accomplished by the 4S pathway, consisting of two monooxygenases, DszC and DszA, and one desulfinase, DszB, which are encoded by the dsz operon
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
the enzyme plays an important role in building up the glycans, which are attached to the S-layer and the flagellin proteins
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
the activated form of sulfoquinovose is required for its incorporation into glycoconjugates
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
final hydride transfer occurs to C-4 rather than C-6 of the enone form of UDP-4-dehydro-D-glucose, leaving this carbon accessible for the subsequent addition of sulfite
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
the activated form of sulfoquinovose is required for its incorporation into glycoconjugates
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
final hydride transfer occurs to C-4 rather than C-6 of the enone form of UDP-4-dehydro-D-glucose, leaving this carbon accessible for the subsequent addition of sulfite
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
-
?
UDP-glucose + sulfite
UDP-6-sulfoquinovose + H2O
key enzyme in formation of the sulfolipid head group precursor UDP-sulfoquinovose, sulfoquinovosyldiacylglycerol is a polar lipid present in photosynthetic membranes, enzyme is complexed in vivo with accessory proteins
-
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
-
increase in the relative amount of sulfolipid under phosphate limitation caused by increased gene expression
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
-
sulfolipid biosynthesis
-
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
sulfolipid biosynthesis
-
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
sulfolipid biosynthesis
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-sulfoquinovopyranose + H2O
UDP-alpha-D-glucose + sulfite
the enzyme catalyzes the reverse reaction
-
-
?
UDP-glucose + ?
UDP-sulfoquinovose + H2O
-
first step of sulfolipid biosynthesis, unknown sulfur donor
-
?
UDP-glucose + sulfite
UDP-6-sulfoquinovose + H2O
key enzyme in formation of the sulfolipid head group precursor UDP-sulfoquinovose, sulfoquinovosyldiacylglycerol is a polar lipid present in photosynthetic membranes, enzyme is complexed in vivo with accessory proteins
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
-
-
-
?
2-hydroxybiphenyl + sulfite
2'-hydroxybiphenyl-2-sulfinate + H2O
-
the microbial conversion of DBT into 2-HBP is accomplished by the 4S pathway, consisting of two monooxygenases, DszC and DszA, and one desulfinase, DszB, which are encoded by the dsz operon
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
the enzyme plays an important role in building up the glycans, which are attached to the S-layer and the flagellin proteins
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
the activated form of sulfoquinovose is required for its incorporation into glycoconjugates
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
the activated form of sulfoquinovose is required for its incorporation into glycoconjugates
-
-
?
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
-
-
-
-
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
-
sulfolipid biosynthesis
-
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
sulfolipid biosynthesis
-
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
sulfolipid biosynthesis
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
tightly bound, enzyme binds 1 NAD+ per monomer, side-chain chemistry and hydrogen-bonding patterns in the NAD+ site
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
sulfate, APS, PAPS, sulfite, thiosulfate, sufide or sulfoglutathione are tested to determine whether they could stimulate the formation of UDP-sulfoquinovose
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Km values for UDP-glucose are indistinguishable for the native and the recombinant enzyme, but the Km value for sulfite is over 4fold lower for the native enzyme
-
additional information
additional information
-
Km values for UDP-glucose are indistinguishable for the native and the recombinant enzyme, but the Km value for sulfite is over 4fold lower for the native enzyme
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
desulfurization activity in strain CECT5279 over time in vivo
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
pH 7.0: about 50% of maximal activity, pH 10.0: about 35% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene agl3, or Saci0423, of the sulfoquinovose biosynthesis operon
-
-
brenda
gene agl3, or Saci0423, of the sulfoquinovose biosynthesis operon
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
SQD1 is a plastid UDP-glucose pyrophosphorylase
brenda
native SoSQD1 is primarily present in the stroma
brenda
-
SQDG1 is a soluble plastid UDP-glucose pyrophosphorylase
brenda
-
SQD1 is a soluble plastid UDP-glucose pyrophosphorylase
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
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
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
-
metabolism
the enzyme is critical for biosynthesis of UDP-sulfoquinovose
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
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
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
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
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
metabolism
-
the enzyme is critical for biosynthesis of UDP-sulfoquinovose
-
physiological function
-
UDP-sulfoquinovose synthase, SqdB, is crucial for sulfolipid synthesis in the purple bacterium
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
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
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
Show AA Sequence and Transmembrane Helices (370 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
250000
250000
native enzyme in a complex with accessory proteins, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion results in bipyramidal crystals, C-2-symmetric homodimer, the protein has a bidomain structure, catalytic site is located in the cleft formed between the two lobes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T145A
E147A
strongly impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
K186A
impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
T144A
mutant enzyme with fully retained activity, conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
Y148A
strongly impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
Y182A
impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
E147A
-
strongly impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
-
K186A
-
impaired conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
-
T144A
-
mutant enzyme with fully retained activity, conversion of UDP-D-glucose to UDP-D-glucose-5,6-ene
-
additional information
T145A
-
greatly reduced activity, site-directed mutagenesis, plays critical role for catalytic activity
additional information
the function of different amino acids in reaction/binding process is analysed, Thr-145, Tyr-182 and Lys-186 are found to fulfill analogous mechanistic roles
additional information
-
construction of a agl3DELTA deletion mutant strain, that shows a significant change in the size of the S-layer SlaA and the flagellin FlaB glycoproteins, with a changed SlaA glycan composition, phenotype, overview. Change in the phenotype under environmental stress conditions
additional information
construction of a agl3DELTA deletion mutant strain, that shows a significant change in the size of the S-layer SlaA and the flagellin FlaB glycoproteins, with a changed SlaA glycan composition, phenotype, overview. Change in the phenotype under environmental stress conditions
additional information
-
construction of a agl3DELTA deletion mutant strain, that shows a significant change in the size of the S-layer SlaA and the flagellin FlaB glycoproteins, with a changed SlaA glycan composition, phenotype, overview. Change in the phenotype under environmental stress conditions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from chloroplasts, recombinant enzyme from Escherichia coli
native enzyme from the chloroplast stroma. Ferredoxin-dependent glutamate synthase, FdGOGAT, co-purifies and is tightly associated with SQD1
-
Ni2+-nitrilotriacetic acid column
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
gene agl3, DNA sequencing and analysis of gene agl3 as part of a gene cluster involved in the biosynthesis of sulfoquinovose and important for the assembly of the S-layer N-glycans, expression in Sulfolobus solfataricus agl3 deletion mutant under the control of a maltose inducible promoter using vector pSVA1450, the expression of agl3 leads to the restoration of the production of full-length glycan
gene dszB, DszB expression pattern in Pseudomonas putida strain CECT5279
-
gene dszB, organized in the dsz operon, DNA and amino acid sequence determination and analysis, genetic organization and expression analysis, recombinant expression in recombinant Rhodococcus erythropolis strain CGMCC 4.1491, that is dsz-deficient
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
SQD1 transcript and protein levels are significantly up-regulated in response to sulfite injection into leaves of dark-stressed wild-type plants or into wild-type and SO Ri mutant leaves grown under a natural light regimes
the UDP-sulfoquinovose synthase in Solanum lycopersicum wild-type leaves is are downregulated during extended darkness, the expression of chloroplast-localized SQD1 transcript decreases during dark stress and recovers upon return to light in both wild-type and SO Ri plant. SQD1 transcript and protein levels are significantly up-regulated in response to sulfite injection into leaves of dark-stressed wild-type plants or into wild-type and SO Ri mutant leaves grown under a natural light regimes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
energy production
environmental protection
medicine
-
sulfolipids, in which synthesis the enzyme is involved, promise anti-tumor and anti-HIV therapeutics based on their inhibition of DNA polymerase and reverse transcriptase
energy production
-
the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
energy production
-
the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
energy production
-
the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
-
environmental protection
-
the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
environmental protection
-
the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
environmental protection
-
the enzyme is useful in biodesulfurization, in which microorganisms selectively remove sulfur atoms from organosulfur compounds, a viable technology to complement the traditional hydrodesulfurization of fuels
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sanda, S.; Leustek, T.; Theisen, M.J.; Garavito, R.M.; Benning, C.
Recombinant Arabidopsis SQD1 converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose in vitro
J. Biol. Chem.
276
3941-3946
2001
Arabidopsis thaliana, Arabidopsis sp.
brenda
Mulichak, A.M.; Theisen, M.J.; Essigmann, B.; Benning, C.; Garavito, R.M.
Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sufolipid headgroup donor UDP-sulfoquinovose
Proc. Natl. Acad. Sci. USA
96
13097-13102
1999
Arabidopsis thaliana (O48917)
brenda
Essigmann, B.; Guler, S.; Narang, R.A.; Linke, D.; Benning, C.
Phosphate availability affects the thylakoid lipid composition and the expression of SQD1, a gene required for sulfolipid biosynthesis in Arabidopsis thaliane
Proc. Natl. Acad. Sci. USA
95
1950-1955
1998
Arabidopsis thaliana (O48917)
brenda
Essigmann, B.; Hespenheide, B.M.; Kuhn, L.A.; Benning, C.
Prediction of the active-site structure and NAD+ binding in SQD1, a protein essential for sulfolipid biosynthesis in Arabidopsis
Arch. Biochem. Biophys.
369
30-41
1999
Arabidopsis thaliana
brenda
Shimojima, M.; Benning, C.
Native uridine 5'-diphosphate-sulfoquinovose synthase, SQD1, from spinach purified as a 250-kDa complex
Arch. Biochem. Biophys.
413
123-130
2003
Spinacia oleracea (Q84KI6), Spinacia oleracea
brenda
Sato, N.; Sugimoto, K.; Meguro, A.; Tsuzuki, M.
Identification of a gene for UDP-sulfoquinovose synthase of a green alga, Chlamydomonas reinhardtii, and its phylogeny
DNA Res.
10
229-237
2003
Chlamydomonas reinhardtii
brenda
Li, G.Q.; Li, S.S.; Zhang, M.L.; Wang, J.; Zhu, L.; Liang, F.L.; Liu, R.L.; Ma, T.
Genetic rearrangement strategy for optimizing the dibenzothiophene biodesulfurization pathway in Rhodococcus erythropolis
Appl. Environ. Microbiol.
74
971-976
2008
Rhodococcus erythropolis
brenda
Calzada, J.; Zamarro, M.T.; Alcon, A.; Santos, V.E.; Diaz, E.; Garcia, J.L.; Garcia-Ochoa, F.
Analysis of dibenzothiophene desulfurization in a recombinant Pseudomonas putida strain
Appl. Environ. Microbiol.
75
875-877
2009
Pseudomonas putida, Pseudomonas putida CECT 5279
brenda
Meyer, B.H.; Zolghadr, B.; Peyfoon, E.; Pabst, M.; Panico, M.; Morris, H.R.; Haslam, S.M.; Messner, P.; Schaeffer, C.; Dell, A.; Albers, S.V.
Sulfoquinovose synthase - an important enzyme in the N-glycosylation pathway of Sulfolobus acidocaldarius
Mol. Microbiol.
82
1150-1163
2011
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius (Q4JBJ3), Sulfolobus acidocaldarius MW001
brenda
Shimojima, M.
Biosynthesis and functions of the plant sulfolipid
Prog. Lipid Res.
50
234-239
2011
Arabidopsis thaliana, Chlamydomonas reinhardtii, Cereibacter sphaeroides, Spinacia oleracea
brenda
Brychkova, G.; Grishkevich, V.; Fluhr, R.; Sagi, M.
An essential role for tomato sulfite oxidase and enzymes of the sulfite network in maintaining leaf sulfite homeostasis
Plant Physiol.
161
148-164
2013
Solanum lycopersicum (C0LIR3), Solanum lycopersicum
brenda
Zolghadr, B.; Gasselhuber, B.; Windwarder, M.; Pabst, M.; Kracher, D.; Kerndl, M.; Zayni, S.; Hofinger-Horvath, A.; Ludwig, R.; Haltrich, D.; Oostenbrink, C.; Obinger, C.; Kosma, P.; Messner, P.; Schffer, C.
UDP-sulfoquinovose formation by Sulfolobus acidocaldarius
Extremophiles
19
451-467
2015
Sulfolobus acidocaldarius (Q4JBJ3), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (Q4JBJ3)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.13.1.1)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
