A0A1T1AUM3 · A0A1T1AUM3_RHOFE
- ProteinDual-specificity RNA methyltransferase RlmN
- GenerlmN
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids382 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Miscellaneous
Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue.
Catalytic activity
- adenosine2503 in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine2503 in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine
RHEA-COMP:10152 CHEBI:74411 Position: 2503+ 2 RHEA-COMP:10001 + 2 CHEBI:59789 = RHEA-COMP:10282 CHEBI:74497 Position: 2503+ CHEBI:17319 + CHEBI:57844 + 2 RHEA-COMP:10000 + CHEBI:57856
Cofactor
Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 91 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 111 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 115 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 118 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 165-166 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GE | ||||||
Binding site | 197 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 219-221 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: SLH | ||||||
Binding site | 301 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 344 | S-methylcysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | rRNA (adenine(2503)-C2-)-methyltransferase activity | |
Molecular Function | rRNA binding | |
Molecular Function | tRNA (adenine(37)-C2)-methyltransferase activity | |
Molecular Function | tRNA binding | |
Biological Process | rRNA base methylation | |
Biological Process | tRNA methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDual-specificity RNA methyltransferase RlmN
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Rhodoferax
Accessions
- Primary accessionA0A1T1AUM3
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 97-339 | Radical SAM core | ||||
Sequence: EDDRGTLCLSTQAGCAMGCRFCSTGHQGFSRNLTTGEIIAQLWFAEHFLRKHLKRDERVISNTVMMGMGEPLQNYSALIPALRMMLDDHGYGLSRRRVTVSTSGLVKKMDLLGVECPVALAVSLHAPNNALRDYLVPLNIKHPLEELMPACVNYLEHAPRDFITFEYCMLDAVNDSDAQAQELVQLVKKYRNSVSWCKFNLIPFNPFPASGLHRSKPERVQGFAKILSEAGITTTVRKTRGDD |
Sequence similarities
Belongs to the radical SAM superfamily. RlmN family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length382
- Mass (Da)42,633
- Last updated2017-05-10 v1
- Checksum9EB6392DA0DCCC3C
Keywords
- Technical term