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Aldolase/RraA
Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein [1]. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing [2]. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions [1]. [1]. 24359411. Biochemical and structural analysis of RraA proteins to decipher. their relationships with. 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipa. te aldolases.. Mazurkewich S, Wang W, Seah SY;. Biochemistry. 2014;53:542-553.. [2]. 14499605. The X-ray structure of Escherichia coli RraA (MenG), A protein. inhibitor of RNA processing.. Monzingo AF, Gao J, Qiu J, Georgiou G, Robertus JD;. J Mol Biol. 2003;332:1015-1024. (from Pfam)
RraA family
The E. coli member of this family has been characterized as a regulator of RNase E [1] and its crystal structure has been analyzed [2]. This model was initially classified as a "hypothetical equivalog" expressing the tentative hypothesis that all members might have the same function as the E. coli enzyme. Considering the second clade of enterobacterial sequences within this family, that appears to be less tenable. The function of these sequences outside of the narrow RraA equivalog model (TIGR02998) remains obscure. All of these were initially annotated as MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error [2,3] in the case of the E. coli protein.
RraA family protein
RraA family protein such as regulator of ribonuclease activity A (RraA), which globally modulates RNA abundance by binding to RNase E and regulating its endonucleolytic activity, and 4-hydroxy-4-methyl-2-oxoglutarate (HMG) aldolase, which catalyzes the aldol cleavage of HMG into 2 molecules of pyruvate
ribonuclease E activity regulator RraA
This family includes a number of closely related sequences from certain enterobacteria. The E. coli member of this family has been characterized as a regulator of RNase E [1] and its crystal structure has been analyzed [2]. The broader subfamily which includes this equivalog, TIGR01935, was initially classified as a "hypothetical equivalog" with the name "regulator of ribonuclease activity A" based on the same evidence for this model. It now appears that, considering the second group of enterobacterial sequences within TIGR01935, the functional assignment is unsupported. THIS PROTEIN IS _NOT_ MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error [2,3].
Regulator of RNase E; increases half-life and abundance of RNAs; interacts with RNase E
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