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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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MetaCyc Enzyme: APS reductase

Species: Thiobacillus denitrificans

Subunit composition of APS reductase = [AprA][AprB]
         APS reductase α subunit = AprA
         APS reductase β subunit = AprB

Summary:
APS reductase enzymes were purified from four different organisms (Archaeoglobus fulgidus, Desulfovibrio desulfuricans, Desulfovibrio vulgaris and Thiobacillus denitrificans) and were found to be very similar to each other despite the fact that these organisms include an archaeon, two sulfate-reducing bacteria, and a sulfur-oxidizing bacterium. In all cases, the enzyme was a heterodimer, composed of a 75 kDa FAD-containing α subunit and a 20 kDa β subunit that contained two a [4Fe-4S] iron-sulfur cluster located in close proximity.

Based on their data the authors proposed that formation of APS from sulfite and AMP occurs at the FAD site followed by electron transfer to a [4Fe-4S] iron-sulfur cluster I.

Based on the similarity of the sequences of dissimilatory APS reductases and sulfite reductases, the authors suggested that these enzymes were present in a last common ancestor of archaea, bacteria and eukarya [Fritz00].

Molecular Weight: 95 kD (experimental) [Fritz00 ]

Gene-Reaction Schematic: ?

Credits:
Created 11-Sep-2006 by Caspi R , SRI International


Enzymatic reaction of: APS reductase

EC Number: 1.8.99.2

sulfite + AMP + an oxidized electron acceptor + 2 H+ <=> adenosine 5'-phosphosulfate + a reduced electron acceptor

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: sulfite oxidation II , sulfite oxidation III

Cofactors or Prosthetic Groups: a [4Fe-4S] iron-sulfur cluster [Fritz00], FAD [Fritz00]


Subunit of APS reductase: APS reductase α subunit

Synonyms: AprA

Gene: aprA Accession Number: G-9573 (MetaCyc)

Molecular Weight: 75.301 kD (from nucleotide sequence)

Molecular Weight: 75 kD (experimental) [Fritz00]

Unification Links: Protein Model Portal:Q5VLA6 , UniProt:Q5VLA6

Relationship Links: InterPro:IN-FAMILY:IPR003953 , InterPro:IN-FAMILY:IPR011803 , InterPro:IN-FAMILY:IPR015939 , InterPro:IN-FAMILY:IPR027477 , Pfam:IN-FAMILY:PF00890


Subunit of APS reductase: APS reductase β subunit

Synonyms: AprB

Gene: aprB Accession Number: G-9574 (MetaCyc)

Molecular Weight: 17.786 kD (from nucleotide sequence)

Molecular Weight: 20 kD (experimental) [Fritz00]

Unification Links: Protein Model Portal:Q5VLA7 , SMR:Q5VLA7 , UniProt:Q5VLA7

Relationship Links: InterPro:IN-FAMILY:IPR011802 , InterPro:IN-FAMILY:IPR017896 , InterPro:IN-FAMILY:IPR017900 , InterPro:IN-FAMILY:IPR022738 , Pfam:IN-FAMILY:PF12139 , Pfam:IN-FAMILY:PF13187 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51379


References

Fritz00: Fritz G, Buchert T, Huber H, Stetter KO, Kroneck PM (2000). "Adenylylsulfate reductases from archaea and bacteria are 1:1 alphabeta-heterodimeric iron-sulfur flavoenzymes--high similarity of molecular properties emphasizes their central role in sulfur metabolism." FEBS Lett 473(1);63-6. PMID: 10802060

Park06: Park YJ, Yoo CB, Choi SY, Lee HB (2006). "Purifications and characterizations of a ferredoxin and its related 2-oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon, Sulfolobus solfataricus P1." J Biochem Mol Biol 39(1);46-54. PMID: 16466637


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc14.