Detail Information for IndEnz0002009534
IED ID IndEnz0002009534
Enzyme Type ID protease009534
Protein Name Ribosomal large subunit pseudouridine synthase D
EC 5.4.99.23
23S rRNA pseudouridine
1911/1915/1917
synthase
rRNA pseudouridylate synthase D
rRNA-uridine isomerase D
Gene Name rluD sfhB yfiI b2594 JW2576
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MAQRVQLTATVSENQLGQRLDQALAEMFPDYSRSRIKEWILDQRVLVNGKVCDKPKEKVLGGEQVAINAEIEEEARFEPQDIPLDIVYEDEDIIIINKPRDLVVHPGAGNPDGTVLNALLHYYPPIADVPRAGIVHRLDKDTTGLMVVAKTVPAQTRLVESLQRREITREYEAVAIGHMTAGGTVDEPISRHPTKRTHMAVHPMGKPAVTHYRIMEHFRVHTRLRLRLETGRTHQIRVHMAHITHPLVGDPVYGGRPRPPKGASEAFISTLRKFDRQALHATMLRLYHPISGIEMEWHAPIPQDMVELIEVMRADFEEHKDEVDWL
Enzyme Length 326
Uniprot Accession Number P33643
Absorption
Active Site ACT_SITE 139
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=uridine(1911/1915/1917) in 23S rRNA = pseudouridine(1911/1915/1917) in 23S rRNA; Xref=Rhea:RHEA:42524, Rhea:RHEA-COMP:10097, Rhea:RHEA-COMP:10098, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.23; Evidence={ECO:0000269|PubMed:11087118, ECO:0000269|PubMed:17937767};
DNA Binding
EC Number 5.4.99.23
Enzyme Function FUNCTION: Responsible for synthesis of pseudouridine from uracil at positions 1911, 1915 and 1917 in 23S ribosomal RNA. Isomerization occurs as a late step during the assembly of the large ribosomal subunit. {ECO:0000269|PubMed:11087118, ECO:0000269|PubMed:17937767}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (15); Chain (1); Domain (1); Frameshift (1); Helix (10); Initiator methionine (1); Mutagenesis (1); Sequence conflict (1); Turn (2)
Keywords 3D-structure;Direct protein sequencing;Isomerase;RNA-binding;Reference proteome;rRNA processing
Interact With P21165; P0A8A4
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D Electron microscopy (1); X-ray crystallography (4)
Cross Reference PDB 1PRZ; 1QYU; 1V9F; 2IST; 7BL5;
Mapped Pubmed ID 14659742; 14730022; 15078091; 15690043; 16606699; 33639093;
Motif
Gene Encoded By
Mass 37,122
Kinetics
Metal Binding
Rhea ID RHEA:42524
Cross Reference Brenda 5.4.99.23;