HMM Summary Page: TIGR02060

Functionadenylylsulfate reductase, beta subunit
Gene SymbolaprB
Trusted Cutoff135.65
Domain Trusted Cutoff135.65
Noise Cutoff55.15
Domain Noise Cutoff55.15
Isology Typeequivalog
EC Number1.8.99.2
HMM Length132
Mainrole CategoryCentral intermediary metabolism
Subrole CategorySulfur metabolism
Gene Ontology TermGO:0009973: adenylyl-sulfate reductase activity molecular_function
GO:0019420: dissimilatory sulfate reduction biological_process
GO:0019425: sulfur oxidation, using siroheme sulfite reductase biological_process
AuthorBrinkac L
Entry DateNov 21 2003 4:08PM
Last ModifiedFeb 14 2011 3:27PM
CommentDuring 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.
ReferencesRN [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 PropertyGenProp0155: dissimilatory sulfate reduction (HMM)