|Function||adenylylsulfate reductase, alpha subunit|
|Domain Trusted Cutoff||641.75|
|Domain Noise Cutoff||326.00|
|Mainrole Category||Central intermediary metabolism|
|Subrole Category||Sulfur metabolism|
|Gene Ontology Term||GO:0009973: adenylyl-sulfate reductase activity molecular_function|
| ||GO:0019420: dissimilatory sulfate reduction biological_process|
| ||GO:0019425: sulfur oxidation, using siroheme sulfite reductase biological_process|
|Entry Date||Nov 24 2003 3:29PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||During dissimilatory sulfate reduction or sulfur oxidation, adenylylsulfate (APS) reductase catalyzes reversibly the two-electron reduction of APS to sulfite and AMP . Found in several bacterial lineages and in Archaeoglobales, APS reductase is a heterodimer composed of an alpha subunit containing a noncovalently bound FAD, and a beta subunit containing two [4Fe-4S] clusters . Described by this model is the alpha subunit of APS reductase, sharing common evolutionary origin with fumarate reductase/succinate dehydrogenase flavoproteins.|
RT 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.
RA Fritz G, Buchert T, Huber H, Stetter KO, Kroneck PM.
RL FEBS Lett. 2000 May 4;473(1):63-6.
DR PFAM; PF02910; Fumarate reductase/succinate dehydrogenase flavoprotein C-terminal domain
DR PFAM; PF00890; FAD binding domain
DR EXPERIMENTAL; GP|2576391; Allochromatium vinosum; insertional inactivation resulted in inability to synthesize APS from sulfite and AMP.
DR EXPERIMENTAL; GP|2648887; Archaeoglobus fulgidus; purified by chromatography, with APS reductase activity measured by spectroscopy.
DR OUTGROUP; GP|2649111; Archaeoglobus fulgidus DSM4304; fumarate reductase, flavoprotein subunit.|
|Genome Property||GenProp0155: dissimilatory sulfate reduction (HMM)|
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