|Function||adenylylsulfate reductase, beta subunit|
|Domain Trusted Cutoff||135.65|
|Domain Noise Cutoff||55.15|
|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 21 2003 4:08PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||During dissimilatory sulfate reduction and 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 beta subunit of APS reductase, sharing common evolutionary origin with other iron-sulfur cluster-binding proteins.|
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; PF00037; iron-sulfur cluster-binding protein
DR EXPERIMENTAL; GP|2576390; Allochromatium vinosum; insertional inactivation resulted in inability to synthesize APS from sulfite and AMP.
DR EXPERIMENTAL; GP|443816; Archaeoglobus fulgidus; purified by chromatography, with APS reductase activity measured by spectroscopy.
DR OUTGROUP; GP|19916865; Methanosarcina acetivorans str. C2A; polyferredoxin|
|Genome Property||GenProp0155: dissimilatory sulfate reduction (HMM)|
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