<?xml version="1.0" encoding="UTF-8"?>
<compound>
  <version>2.0</version>
  <creation_date>2012-05-31 13:52:54 -0600</creation_date>
  <update_date>2015-09-17 15:41:11 -0600</update_date>
  <accession>ECMDB01448</accession>
  <m2m_id>M2MDB000391</m2m_id>
  <name>Sulfate</name>
  <description>The sulfate ion is a polyatomic anion with the empirical formula SO42- and a molecular mass of 96.06 daltons; it consists of one central sulfur atom surrounded by four equivalent oxygen atoms in a tetrahedral arrangement. The sulfate ion carries a negative two charge and is the conjugate base of the hydrogen sulfate ion, HSO4-, which is the conjugate base of H2SO4, sulfuric acid.    In inorganic chemistry, a sulfate (IUPAC-recommended spelling; also sulphate in British English) is a salt of sulfuric acid.    Sulfate aerosols can act as cloud condensation nuclei and this leads to greater numbers of smaller droplets of water. Lots of smaller droplets can diffuse light more efficiently than just a few larger droplets.</description>
  <synonyms>
    <synonym>H2SO4</synonym>
    <synonym>SO4--</synonym>
    <synonym>SO4-2</synonym>
    <synonym>SO42-</synonym>
    <synonym>SO&lt;SUB&gt;4&lt;/SUB&gt;&lt;SUP&gt;--&lt;/SUP&gt;</synonym>
    <synonym>SO&lt;SUB&gt;4&lt;/SUB&gt;&lt;SUP&gt;-2&lt;/SUP&gt;</synonym>
    <synonym>SO&lt;SUB&gt;4&lt;/SUB&gt;&lt;SUP&gt;2-&lt;/SUP&gt;</synonym>
    <synonym>Sulfate (ion 2-)</synonym>
    <synonym>Sulfate anion</synonym>
    <synonym>Sulfate anion(2-)</synonym>
    <synonym>Sulfate dianion</synonym>
    <synonym>Sulfate ion</synonym>
    <synonym>Sulfate ion (SO42-)</synonym>
    <synonym>Sulfate ion(2-)</synonym>
    <synonym>Sulfate(2-)</synonym>
    <synonym>Sulfuric acid</synonym>
    <synonym>Sulfuric acid (ion 2-)</synonym>
    <synonym>Sulfuric acid anion</synonym>
    <synonym>Sulfuric acid anion(2-)</synonym>
    <synonym>Sulfuric acid dianion</synonym>
    <synonym>Sulfuric acid ion</synonym>
    <synonym>Sulfuric acid ion (so42-)</synonym>
    <synonym>Sulfuric acid ion(2-)</synonym>
    <synonym>Sulfuric acid(2-)</synonym>
    <synonym>Sulphate</synonym>
    <synonym>Sulphate (ion 2-)</synonym>
    <synonym>Sulphate anion</synonym>
    <synonym>Sulphate anion(2-)</synonym>
    <synonym>Sulphate dianion</synonym>
    <synonym>Sulphate ion</synonym>
    <synonym>Sulphate ion (SO42-)</synonym>
    <synonym>Sulphate ion(2-)</synonym>
    <synonym>Sulphate(2-)</synonym>
    <synonym>Sulphuric acid</synonym>
    <synonym>Sulphuric acid (ion 2-)</synonym>
    <synonym>Sulphuric acid anion</synonym>
    <synonym>Sulphuric acid anion(2-)</synonym>
    <synonym>Sulphuric acid dianion</synonym>
    <synonym>Sulphuric acid ion</synonym>
    <synonym>Sulphuric acid ion (so42-)</synonym>
    <synonym>Sulphuric acid ion(2-)</synonym>
    <synonym>Sulphuric acid(2-)</synonym>
  </synonyms>
  <chemical_formula>O4S</chemical_formula>
  <average_molecular_weight>96.063</average_molecular_weight>
  <monisotopic_moleculate_weight>95.951729178</monisotopic_moleculate_weight>
  <iupac_name>sulfuric acid</iupac_name>
  <traditional_iupac>sulfuric acid</traditional_iupac>
  <cas_registry_number>14808-79-8</cas_registry_number>
  <smiles>[O-]S([O-])(=O)=O</smiles>
  <inchi>InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2</inchi>
  <inchikey>QAOWNCQODCNURD-UHFFFAOYSA-L</inchikey>
  <state>Solid</state>
  <cellular_locations>
    <cellular_location>Cytosol</cellular_location>
    <cellular_location>Extra-organism</cellular_location>
    <cellular_location>Periplasm</cellular_location>
  </cellular_locations>
  <predicted_properties>
  </predicted_properties>
  <experimental_properties>
  </experimental_properties>
  <property>
    <kind>logp</kind>
    <value>-0.84</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>pka_strongest_acidic</kind>
    <value>-3</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>iupac</kind>
    <value>sulfuric acid</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>average_mass</kind>
    <value>96.063</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>mono_mass</kind>
    <value>95.951729178</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>smiles</kind>
    <value>[O-]S([O-])(=O)=O</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formula</kind>
    <value>O4S</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchi</kind>
    <value>InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>inchikey</kind>
    <value>QAOWNCQODCNURD-UHFFFAOYSA-L</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polar_surface_area</kind>
    <value>74.6</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>refractivity</kind>
    <value>13.77</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>polarizability</kind>
    <value>6.51</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>rotatable_bond_count</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>acceptor_count</kind>
    <value>4</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>donor_count</kind>
    <value>2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>physiological_charge</kind>
    <value>-2</value>
    <source>ChemAxon</source>
  </property>
  <property>
    <kind>formal_charge</kind>
    <value>0</value>
    <source>ChemAxon</source>
  </property>
  <pathways>
    <pathway>
      <name>Purine metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00230</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Cysteine and methionine metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00270</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Sphingolipid metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00600</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Selenoamino acid metabolism</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00450</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Sulfur metabolism</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and  adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate,  which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. 
The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described.
The third variant of sulfur metabolism starts with the import of an alkyl sulfate into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. The alkyl sulfate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000922</pathwhiz_id>
      <kegg_map_id>ec00920</kegg_map_id>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>Steroid hormone biosynthesis</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec00140</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Microbial metabolism in diverse environments</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec01120</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>ABC transporters</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>ec02010</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Monobactam biosynthesis</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>eco00261</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>Metabolic pathways</name>
      <description/>
      <pathwhiz_id/>
      <kegg_map_id>eco01100</kegg_map_id>
      <subject/>
    </pathway>
    <pathway>
      <name>cysteine biosynthesis</name>
      <description>The pathway of cysteine biosynthesis is a two-step conversion starting from L-serine and yielding L-cysteine. L-serine biosynthesis is shown for context.
L-cysteine can also be synthesized from sulfate derivatives.
The process through L-serine involves a serine acetyltransferase that produces a O-acetylserine which reacts together with hydrogen sulfide through a cysteine synthase complex in order to produce L-cysteine and acetic acid.
Hydrogen sulfide is produced from a sulfate. Sulfate reacts with sulfate adenylyltransferase to produce adenosine phosphosulfate. This compound in turn is phosphorylated through a adenylyl-sulfate kinase into a phosphoadenosine phosphosulfate which in turn reacts with a phosphoadenosine phosphosulfate reductase to produce a sulfite. The sulfite reacts with a sulfite reductase to produce the hydrogen sulfide.
This pathway is regulated at the genetic level in its second step, wtih both cysteine synthase isozymes being under the positive control of the cysteine-responsive transcription factor CysB. It is also subject to very strong feedback inhibition of its first step by the final pathway product, cysteine.

Although two cysteine synthase isozymes exist, only cysteine synthase A (CysK) forms a complex with serine acetyltransferase. CysK is also the only one of the two cysteine synthases that is required for cell viability on cysteine-free medium.

Both steps in this pathway are reversible. Based on genetic and proteomic data, it appears that the cysteine synthases may actually act as a sulfur scavenging system during sulfur starvation, stripping sulfur off of L-cysteine, generating any number of variant amino acids in the process.</description>
      <pathwhiz_id>PW000800</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>inner membrane transport</name>
      <description>list of inner membrane transport complexes, transporting compounds from the periplasmic space to the cytosol
This pathway should be updated regularly with the new inner membrae transports added</description>
      <pathwhiz_id>PW000786</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfur metabolism (butanesulfonate)</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 1-butanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 1-butanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000923</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfur metabolism (ethanesulfonate)</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case ethanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Ethanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000925</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfur metabolism (isethionate)</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case isethionate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Isethionate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000926</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfur metabolism (methanesulfonate)</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case methanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. Methanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and an aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000927</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfur metabolism (propanesulfonate)</name>
      <description>The sulfur metabolism pathway starts in three possible ways. The first is the uptake of sulfate through an active transport reaction via a sulfate transport system containing an ATP-binding protein which hydrolyses ATP. Sulfate is converted by the sulfate adenylyltransferase enzymatic complex to adenosine phosphosulfate through the addition of adenine from a molecule of ATP, along with one phosphate group. Adenosine phosphosulfate is further converted to phoaphoadenosine phosphosulfate through an ATP hydrolysis and dehydrogenation reaction by the adenylyl-sulfate kinase. Phoaphoadenosine phosphosulfate is finally dehydrogenated and converted to sulfite by phosphoadenosine phosphosulfate reductase. This reaction requires magnesium, and adenosine 3',5'-diphosphate is the bi-product. A thioredoxin is also oxidized. Sulfite can also be produced from the dehydrogenation of cyanide along with the conversion of thiosulfate to thiocyanate by the thiosulfate sulfurtransferase enzymatic complex. Sulfite next undergoes a series of reactions that lead to the production of pyruvic acid, which is a precursor for pathways such as gluconeogenesis. The first reaction in this series is the conversion of sulfite to hydrogen sulfide through hygrogenation and the deoxygenation of sulfite to form a water molecule. The reaction is catalyzed by the sulfite reductase [NADPH] flavoprotein alpha and beta components. Siroheme, 4Fe-4S, flavin mononucleotide, and FAD function as cofactors or prosthetic groups. Hydrogen sulfide next undergoes dehydrogenation in a reversible reaction to form L-Cysteine and acetic acid, via the cysteine synthase complex and the coenzyme pyridoxal 5'-phosphate. L-Cysteine is dehydrogenated and converted to 2-aminoacrylic acid (a bronsted acid) and hydrogen sulfide(which may be reused) by a larger enzymatic complex composed of cysteine synthase A/B, protein malY, cystathionine-β-lyase, and tryptophanase, along with the coenzyme pyridoxal 5'-phosphate. 2-aminoacrylic acid isomerizes to 2-iminopropanoate, which along with a water molecule and a hydrogen ion is lastly converted to pyruvic acid and ammonium in a spontaneous fashion. The second possible initial starting point for sulfur metabolism is the import of taurine(an alternate sulfur source) into the cytoplasm via the taurine ABC transporter complex. Taurine, oxoglutaric acid, and oxygen are converted to sulfite by the alpha-ketoglutarate-dependent taurine dioxygenase. Carbon dioxide, succinic acid, and aminoacetaldehyde are bi-products of this reaction. Sulfite next enters pyruvic acid synthesis as already described. The third variant of sulfur metabolism starts with the import of an alkyl sulfate, in this case 3-(N-morpholino)propanesulfonate, into the cytoplasm via an aliphatic sulfonate ABC transporter complex which hydrolyses ATP. 3-(N-morpholino)propanesulfonate is dehydrogenated and along with oxygen is converted to sulfite and betaine aldehyde by the FMNH2-dependent alkanesulfonate monooxygenase enzyme. Water and flavin mononucleotide(which is used in a subsequent reaction as a prosthetic group) are also produced. Sulfite is next converted to pyruvic acid by the process already described.</description>
      <pathwhiz_id>PW000924</pathwhiz_id>
      <kegg_map_id/>
      <subject>Metabolic</subject>
    </pathway>
    <pathway>
      <name>sulfate activation for sulfonation</name>
      <ecocyc_pathway_id>PWY-5340</ecocyc_pathway_id>
    </pathway>
  </pathways>
  <spectra>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>935</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>31783</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::CMs</type>
      <spectrum_id>168848</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>29621</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>29622</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>29623</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>36179</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>36180</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>36181</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>439730</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>439747</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>439820</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>439821</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>449815</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>449816</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>449859</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>449884</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>449919</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>450028</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>450029</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>450030</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>450031</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2429548</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2429549</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2429550</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2506139</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2506140</spectrum_id>
    </spectrum>
    <spectrum>
      <type>Specdb::MsMs</type>
      <spectrum_id>2506141</spectrum_id>
    </spectrum>
  </spectra>
  <hmdb_id>HMDB01448</hmdb_id>
  <pubchem_compound_id>1117</pubchem_compound_id>
  <chemspider_id>1085</chemspider_id>
  <kegg_id>C00059</kegg_id>
  <chebi_id>16189</chebi_id>
  <biocyc_id>SULFATE</biocyc_id>
  <het_id>SUL</het_id>
  <wikipidia>Sulfate</wikipidia>
  <foodb_id/>
  <general_references>
    <reference>
      <reference_text>Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590.</reference_text>
      <pubmed_id>21097882</pubmed_id>
    </reference>
    <reference>
      <reference_text>Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114.</reference_text>
      <pubmed_id>22080510</pubmed_id>
    </reference>
    <reference>
      <reference_text>van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25.</reference_text>
      <pubmed_id>17765195</pubmed_id>
    </reference>
    <reference>
      <reference_text>Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.</reference_text>
      <pubmed_id>18331064</pubmed_id>
    </reference>
  </general_references>
  <synthesis_reference>Zhang, Qiu-Ju; Wang, Xiao; Chen, Jian-Min; Zhuang, Guo-Shun.  Formation of Fe(II) (aq) and sulfate via heterogeneous reaction of SO2 with Fe2O3.    Gaodeng Xuexiao Huaxue Xuebao  (2006),  27(7),  1347-1350.</synthesis_reference>
  <msds_url>http://hmdb.ca/system/metabolites/msds/000/001/310/original/HMDB01448.pdf?1358462055</msds_url>
  <enzymes>
    <enzyme>
      <name>Sulfate/thiosulfate import ATP-binding protein cysA</name>
      <uniprot_id>P16676</uniprot_id>
      <uniprot_name>CYSA_ECOLI</uniprot_name>
      <gene_name>cysA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16676.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate adenylyltransferase subunit 2</name>
      <uniprot_id>P21156</uniprot_id>
      <uniprot_name>CYSD_ECOLI</uniprot_name>
      <gene_name>cysD</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P21156.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate adenylyltransferase subunit 1</name>
      <uniprot_id>P23845</uniprot_id>
      <uniprot_name>CYSN_ECOLI</uniprot_name>
      <gene_name>cysN</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P23845.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Arylsulfatase</name>
      <uniprot_id>P25549</uniprot_id>
      <uniprot_name>ASLA_ECOLI</uniprot_name>
      <gene_name>aslA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P25549.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate transport system permease protein cysW</name>
      <uniprot_id>P0AEB0</uniprot_id>
      <uniprot_name>CYSW_ECOLI</uniprot_name>
      <gene_name>cysW</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AEB0.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Molybdenum transport system permease protein modB</name>
      <uniprot_id>P0AF01</uniprot_id>
      <uniprot_name>MODB_ECOLI</uniprot_name>
      <gene_name>modB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AF01.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate transport system permease protein cysT</name>
      <uniprot_id>P16701</uniprot_id>
      <uniprot_name>CYST_ECOLI</uniprot_name>
      <gene_name>cysU</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16701.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Putative aliphatic sulfonates transport permease protein ssuC</name>
      <uniprot_id>P75851</uniprot_id>
      <uniprot_name>SSUC_ECOLI</uniprot_name>
      <gene_name>ssuC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P75851.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate-binding protein</name>
      <uniprot_id>P0AG78</uniprot_id>
      <uniprot_name>SUBI_ECOLI</uniprot_name>
      <gene_name>sbp</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AG78.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Thiosulfate-binding protein</name>
      <uniprot_id>P16700</uniprot_id>
      <uniprot_name>CYSP_ECOLI</uniprot_name>
      <gene_name>cysP</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16700.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Molybdenum import ATP-binding protein ModC</name>
      <uniprot_id>P09833</uniprot_id>
      <uniprot_name>MODC_ECOLI</uniprot_name>
      <gene_name>modC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P09833.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Molybdate-binding periplasmic protein</name>
      <uniprot_id>P37329</uniprot_id>
      <uniprot_name>MODA_ECOLI</uniprot_name>
      <gene_name>modA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P37329.xml</protein_url>
    </enzyme>
  </enzymes>
  <transporters>
    <enzyme>
      <name>Sulfate/thiosulfate import ATP-binding protein cysA</name>
      <uniprot_id>P16676</uniprot_id>
      <uniprot_name>CYSA_ECOLI</uniprot_name>
      <gene_name>cysA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16676.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate transport system permease protein cysW</name>
      <uniprot_id>P0AEB0</uniprot_id>
      <uniprot_name>CYSW_ECOLI</uniprot_name>
      <gene_name>cysW</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AEB0.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Molybdenum transport system permease protein modB</name>
      <uniprot_id>P0AF01</uniprot_id>
      <uniprot_name>MODB_ECOLI</uniprot_name>
      <gene_name>modB</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AF01.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Putative sulfate transporter ychM</name>
      <uniprot_id>P0AFR2</uniprot_id>
      <uniprot_name>YCHM_ECOLI</uniprot_name>
      <gene_name>ychM</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AFR2.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate transport system permease protein cysT</name>
      <uniprot_id>P16701</uniprot_id>
      <uniprot_name>CYST_ECOLI</uniprot_name>
      <gene_name>cysU</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16701.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Putative aliphatic sulfonates transport permease protein ssuC</name>
      <uniprot_id>P75851</uniprot_id>
      <uniprot_name>SSUC_ECOLI</uniprot_name>
      <gene_name>ssuC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P75851.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Sulfate-binding protein</name>
      <uniprot_id>P0AG78</uniprot_id>
      <uniprot_name>SUBI_ECOLI</uniprot_name>
      <gene_name>sbp</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P0AG78.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Outer membrane protein N</name>
      <uniprot_id>P77747</uniprot_id>
      <uniprot_name>OMPN_ECOLI</uniprot_name>
      <gene_name>ompN</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P77747.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Thiosulfate-binding protein</name>
      <uniprot_id>P16700</uniprot_id>
      <uniprot_name>CYSP_ECOLI</uniprot_name>
      <gene_name>cysP</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P16700.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Outer membrane pore protein E</name>
      <uniprot_id>P02932</uniprot_id>
      <uniprot_name>PHOE_ECOLI</uniprot_name>
      <gene_name>phoE</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P02932.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Outer membrane protein F</name>
      <uniprot_id>P02931</uniprot_id>
      <uniprot_name>OMPF_ECOLI</uniprot_name>
      <gene_name>ompF</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P02931.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Molybdenum import ATP-binding protein ModC</name>
      <uniprot_id>P09833</uniprot_id>
      <uniprot_name>MODC_ECOLI</uniprot_name>
      <gene_name>modC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P09833.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Outer membrane protein C</name>
      <uniprot_id>P06996</uniprot_id>
      <uniprot_name>OMPC_ECOLI</uniprot_name>
      <gene_name>ompC</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P06996.xml</protein_url>
    </enzyme>
    <enzyme>
      <name>Molybdate-binding periplasmic protein</name>
      <uniprot_id>P37329</uniprot_id>
      <uniprot_name>MODA_ECOLI</uniprot_name>
      <gene_name>modA</gene_name>
      <protein_url>http://ecmdb.ca/proteins/P37329.xml</protein_url>
    </enzyme>
  </transporters>
  <reactions>
    <reaction_text>Adenosine triphosphate + Water + Sulfate &gt; ADP + Hydrogen ion + Phosphate + Sulfate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-70-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Water + Sulfate &gt; ADP + Hydrogen ion + Phosphate + Sulfate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-70-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Guanosine triphosphate + Water + Sulfate &gt; Adenosine phosphosulfate + Guanosine diphosphate + Phosphate + Pyrophosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Sulfate &lt;&gt; Pyrophosphate + Adenosine phosphosulfate</reaction_text>
    <kegg_reaction_id>R00529</kegg_reaction_id>
    <ecocyc_id>SULFATE-ADENYLYLTRANS-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Estrone 3-sulfate + Water &lt;&gt; Sulfate + Estrone</reaction_text>
    <kegg_reaction_id>R03980</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Sulfatide + Water &lt;&gt; Galactosylceramide + Sulfate</reaction_text>
    <kegg_reaction_id>R04856</kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Sulfate + Water + Adenosine triphosphate &gt; Sulfate + Phosphate + ADP + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-70-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Sulfate + Water + Adenosine triphosphate &gt; Sulfate + Phosphate + ADP + Hydrogen ion</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ABC-70-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Water + a phenol sulfate &lt;&gt; Sulfate + a phenol</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>ARYLSULFAT-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Hydrogen ion + Sulfate + Adenosine triphosphate &gt; Adenosine phosphosulfate + Pyrophosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id>SULFATE-ADENYLYLTRANS-RXN</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>A phenol sulfate + Water &gt; a phenol + Sulfate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Sulfate &gt; Pyrophosphate + Adenosine phosphosulfate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>ADP + Phosphate + 4 Hydrogen ion + Heme + Nickel(2+) + Iron chelate + Taurine + Molybdate + Magnesium + Fe3+ + Potassium + Polyamine + vitamin B12 + Sulfate + glycerol-3-phosphate + Phosphonate + D-Maltose &lt;&gt; Adenosine triphosphate +3 Hydrogen ion + Water</reaction_text>
    <kegg_reaction_id>R00086</kegg_reaction_id>
    <ecocyc_id>RXN0-1061</ecocyc_id>
    <pw_reaction_id/>
    <reaction_text>Aryl sulfate + Water &lt;&gt; Phenol + Sulfate</reaction_text>
    <kegg_reaction_id>R01243 </kegg_reaction_id>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Hydrogen ion + Sulfate + Sulfate &gt; Adenosine phosphosulfate + Pyrophosphate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_R002852</pw_reaction_id>
    <reaction_text>Adenosine triphosphate + Water + Sulfate + Sulfate &gt; Adenosine diphosphate + Phosphate + Hydrogen ion + Sulfate + ADP</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id>PW_RCT000145</pw_reaction_id>
    <reaction_text>Adenosine triphosphate + Sulfate &lt;&gt; Pyrophosphate + Adenosine phosphosulfate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
    <reaction_text>Adenosine triphosphate + Sulfate &lt;&gt; Pyrophosphate + Adenosine phosphosulfate</reaction_text>
    <kegg_reaction_id/>
    <ecocyc_id/>
    <pw_reaction_id/>
  </reactions>
  <concentrations>
  </concentrations>
</compound>
