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Information on EC 3.13.1.1 - UDP-sulfoquinovose synthase and Organism(s) Arabidopsis thaliana and UniProt Accession O48917

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EC Tree
     3 Hydrolases
         3.13 Acting on carbon-sulfur bonds
             3.13.1 Acting on carbon-sulfur bonds
                3.13.1.1 UDP-sulfoquinovose synthase
IUBMB 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.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: O48917
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
udp-sulfoquinovose synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfite:UDP-glucose sulfotransferase
-
-
-
-
synthase, uridine diphosphosulfoquinovose
-
-
-
-
UDP-sulfoquinovose synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
show the reaction diagram
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of sulfonic acid
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-
-
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hydrolysis of C-S bond
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-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
337378-74-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
show the reaction diagram
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
show the reaction diagram
-
-
-
-
?
UDP-glucose + ?
UDP-sulfoquinovose + H2O
show the reaction diagram
-
first step of sulfolipid biosynthesis, unknown sulfur donor
-
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
show the reaction diagram
UDP-alpha-D-glucose + sulfite
UDP-alpha-D-sulfoquinovopyranose + H2O
show the reaction diagram
-
-
-
-
?
UDP-glucose + ?
UDP-sulfoquinovose + H2O
show the reaction diagram
-
first step of sulfolipid biosynthesis, unknown sulfur donor
-
?
UDP-glucose + sulfite
UDP-sulfoquinovose + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sulfite
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increasing concentrations beyond 0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
sulfite
-
-
0.15
UDP-glucose
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00167
UDP-glucose
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
SQDG1 is a soluble plastid UDP-glucose pyrophosphorylase
Manually annotated by BRENDA team
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photosynthetic
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SQD1_ARATH
477
0
53114
Swiss-Prot
Chloroplast (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45500
-
recombinant protein, lacking the transit peptide
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 25 mM NaH2PO4, pH 7.5, 300 mM NaCl, 20% glycerol
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4°C, 50 mM MES buffer, pH 6.5, 10 mM UDP-glucose, stable for 10 days
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4°C, 50 mM MES buffer, pH 6.5, stable for 2-3 days
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-nitrilotriacetic acid column
Ni2+-nitrilotriacetic acid column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli
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gene SQD1, recombinant expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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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
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.
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Shimojima, M.
Biosynthesis and functions of the plant sulfolipid
Prog. Lipid Res.
50
234-239
2011
Arabidopsis thaliana, Cereibacter sphaeroides, Chlamydomonas reinhardtii, Spinacia oleracea
Manually annotated by BRENDA team