Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Enzyme: 16S rRNA pseudouridine 516 synthase

Gene: rsuA Accession Numbers: EG12044 (MetaCyc), b2183, ECK2177

Synonyms: yejD

Species: Escherichia coli K-12 substr. MG1655

Summary:
RsuA is the pseudouridine synthase that is responsible for pseudouridylation of 16S rRNA at position 516 [Wrzesinski95, Conrad99]. In vitro, the enzyme does not modify free 16S rRNA. The preferred substrate is a 5'-terminal fragment of 16S rRNA complexed with 30S ribosomal proteins, suggesting that pseudouridylation occurs at an intermediate stage of 30S assembly in vivo [Wrzesinski95].

Crystal structures of RsuA in complex with uracil or UMP have been solved. Despite limited sequence similarity, the structure of RsuA is similar to that of TruA, a tRNA pseudouridine synthase [Sivaraman02].

An rsuA mutation causes a defect in pseudouridylation at position 516 in the 16S rRNA, and a D102N or D102T mutation at a conserved aspartate was shown to cause a defect in catalytic activity [Conrad99]. An rsuA mutant does not exhibit any obvious growth defect [Conrad99].

Reviews: [Hamma06, Hur06]

Locations: cytosol

Map Position: [2,277,810 <- 2,278,505]

Molecular Weight of Polypeptide: 25.865 kD (from nucleotide sequence), 32.5 kD (experimental) [Wrzesinski95 ]

Unification Links: ASAP:ABE-0007223 , CGSC:36034 , DIP:DIP-35902N , EchoBASE:EB1978 , EcoGene:EG12044 , EcoliWiki:b2183 , Mint:MINT-1221744 , ModBase:P0AA43 , OU-Microarray:b2183 , PortEco:rsuA , PR:PRO_000023891 , Pride:P0AA43 , Protein Model Portal:P0AA43 , RefSeq:NP_416688 , RegulonDB:EG12044 , SMR:P0AA43 , String:511145.b2183 , UniProt:P0AA43

Relationship Links: InterPro:IN-FAMILY:IPR000748 , InterPro:IN-FAMILY:IPR002942 , InterPro:IN-FAMILY:IPR006145 , InterPro:IN-FAMILY:IPR018496 , InterPro:IN-FAMILY:IPR020103 , PDB:Structure:1KSK , PDB:Structure:1KSL , PDB:Structure:1KSV , Pfam:IN-FAMILY:PF00849 , Pfam:IN-FAMILY:PF01479 , Prosite:IN-FAMILY:PS01149 , Prosite:IN-FAMILY:PS50889 , Smart:IN-FAMILY:SM00363

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0000455 - enzyme-directed rRNA pseudouridine synthesis Inferred from experiment [Conrad99]
GO:0001522 - pseudouridine synthesis Inferred by computational analysis [GOA01]
GO:0006364 - rRNA processing Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Butland05]
GO:0009982 - pseudouridine synthase activity Inferred from experiment Inferred by computational analysis [GOA01, Wrzesinski95]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016853 - isomerase activity Inferred by computational analysis [UniProtGOA11]
GO:0016866 - intramolecular transferase activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm

MultiFun Terms: information transfer RNA related RNA modification

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: 16S rRNA pseudouridine synthase (16S rRNA pseudouridine 516 synthase)

EC Number: 5.4.99.19

a uridine516 in 16S rRNA <=> a 16S rRNA pseudouridine516

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Sequence Features

Feature Class Location Common Name Citations Comment
Conserved-Region 1 -> 68  
[UniProt09]
UniProt: S4 RNA-binding;
Mutagenesis-Variant 102  
[Conrad99, UniProt11]
Alternate sequence: T; UniProt: Loss of activity.
Alternate sequence: N; UniProt: Loss of activity.
Active-Site 102 catalytic aspartate residue
[Conrad99]
 

History:
10/20/97 Gene b2183 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12044; confirmed by SwissProt match.


References

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Conrad99: Conrad J, Niu L, Rudd K, Lane BG, Ofengand J (1999). "16S ribosomal RNA pseudouridine synthase RsuA of Escherichia coli: deletion, mutation of the conserved Asp102 residue, and sequence comparison among all other pseudouridine synthases." RNA 5(6);751-63. PMID: 10376875

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Hamma06: Hamma T, Ferre-D'Amare AR (2006). "Pseudouridine synthases." Chem Biol 13(11);1125-35. PMID: 17113994

Hur06: Hur S, Stroud RM, Finer-Moore J (2006). "Substrate recognition by RNA 5-methyluridine methyltransferases and pseudouridine synthases: a structural perspective." J Biol Chem 281(51);38969-73. PMID: 17085441

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Sivaraman02: Sivaraman J, Sauve V, Larocque R, Stura EA, Schrag JD, Cygler M, Matte A (2002). "Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP." Nat Struct Biol 9(5);353-8. PMID: 11953756

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Wrzesinski95: Wrzesinski J, Bakin A, Nurse K, Lane BG, Ofengand J (1995). "Purification, cloning, and properties of the 16S RNA pseudouridine 516 synthase from Escherichia coli." Biochemistry 34(27);8904-13. PMID: 7612632


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Wed Nov 26, 2014, biocyc13.