ExplorEnz: EC 5.4.99.29

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5.4.99.29

Accepted name:

23S rRNA pseudouridine⁷⁴⁶ synthase

Reaction:

23S rRNA uridine⁷⁴⁶ = 23S rRNA pseudouridine⁷⁴⁶

Other name(s):

RluA (ambiguous); 23S RNA PSI746 synthase; 23S rRNA pseudouridine synthase; pseudouridine synthase RluA (ambiguous)

Systematic name:

23S rRNA-uridine⁷⁴⁶ uracil mutase

Comments:

RluA is the sole protein responsible for the in vivo formation of 23S RNA pseudouridine⁷⁴⁶ [2]. The dual-specificity enzyme also catalyses the formation of uridine³² in tRNA [3]. cf. EC 5.4.99.28 (tRNA pseudouridine³² synthase).

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Hoang, C., Chen, J., Vizthum, C.A., Kandel, J.M., Hamilton, C.S., Mueller, E.G. and Ferre-D'Amare, A.R. Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure. Mol. Cell 24 (2006) 535–545. [DOI] [PMID: 17188032]
2.	Raychaudhuri, S., Niu, L., Conrad, J., Lane, B.G. and Ofengand, J. Functional effect of deletion and mutation of the Escherichia coli ribosomal RNA and tRNA pseudouridine synthase RluA. J. Biol. Chem. 274 (1999) 18880–18886. [DOI] [PMID: 10383384]
3.	Wrzesinski, J., Nurse, K., Bakin, A., Lane, B.G. and Ofengand, J. A dual-specificity pseudouridine synthase: an Escherichia coli synthase purified and cloned on the basis of its specificity for Ψ⁷⁴⁶ in 23S RNA is also specific for Ψ³² in tRNA^Phe. RNA 1 (1995) 437–448. [PMID: 7493321]

[EC 5.4.99.29 created 2011]