Accession | TIGR02060 |
Name | aprB |
Function | adenylylsulfate reductase, beta subunit |
Gene Symbol | aprB |
Trusted Cutoff | 135.65 |
Domain Trusted Cutoff | 135.65 |
Noise Cutoff | 55.15 |
Domain Noise Cutoff | 55.15 |
Isology Type | equivalog |
EC Number | 1.8.99.2 |
HMM Length | 132 |
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 |
Author | Brinkac L |
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 [1]. 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 [1]. Described by this model is the beta subunit of APS reductase, sharing common evolutionary origin with other iron-sulfur cluster-binding proteins. |
References | RN [1]
RM 10802060
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) |