Species: Thiobacillus denitrificans
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]
Enzymatic reaction of: APS reductase
EC Number: 188.8.131.52sulfite + AMP + an oxidized unknown electron acceptor + 2 H+ → adenosine 5'-phosphosulfate + an reduced unknown electron acceptor
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
This reaction is reversible.
|Gene:||aprA||Accession Number: G-9573 (MetaCyc)|
Molecular Weight: 75.301 kD (from nucleotide sequence)
Molecular Weight: 75 kD (experimental) [Fritz00]
|Gene:||aprB||Accession Number: G-9574 (MetaCyc)|
Molecular Weight: 17.786 kD (from nucleotide sequence)
Molecular Weight: 20 kD (experimental) [Fritz00]
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
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
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