P0A176 · MNME_PSEPU
- ProteintRNA modification GTPase MnmE
- GenemnmE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids456 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm5s2U34.
Cofactor
Note: Binds 1 potassium ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 24 | (6S)-5-formyl-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 81 | (6S)-5-formyl-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 120 | (6S)-5-formyl-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 226 | K+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 226-231 | GTP (UniProtKB | ChEBI) | ||||
Sequence: NAGKSS | ||||||
Binding site | 230 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 245 | K+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 245-251 | GTP (UniProtKB | ChEBI) | ||||
Sequence: TDIAGTT | ||||||
Binding site | 247 | K+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 250 | K+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 251 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 270-273 | GTP (UniProtKB | ChEBI) | ||||
Sequence: DTAG | ||||||
Binding site | 335-338 | GTP (UniProtKB | ChEBI) | ||||
Sequence: NKAD | ||||||
Binding site | 456 | (6S)-5-formyl-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | metal ion binding | |
Biological Process | tRNA methylation | |
Biological Process | tRNA wobble uridine modification |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nametRNA modification GTPase MnmE
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionP0A176
- Secondary accessions
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000188906 | 1-456 | tRNA modification GTPase MnmE | |||
Sequence: MNTVRETIAAIATAQGRGGVGIVRLSGPLAAKAGLLITGRTLTPRHAHYGPFRDDEGLVLDEGIALFFPGPNSFTGEDVLELQGHGGPVVLDMLLQRCVQVGCRLARPGEFSERAFLNDKLDLAQAEAIADLIEASSSQAARNALRSLQGEFSRRVHSLTEALIALRIYVEAAIDFPEEEIDFLADGHVLSMLDAVRSELSTVQREAGQGALLRDGMTVVIAGRPNAGKSSLLNQLAGREAAIVTDIAGTTRDILREHIHIDGMPLHVVDTAGLRDTDDHVEKIGVERALKAIGEADRVLLVVDSTAPEASDPFALWPEFLAQRPDPAKVTLIRNKADLSGERVALEQCDDGHVTITLSAKGDDTGLQLLRDHLKGCMGYEQTAESGFSARRRHLDALRQASEHLEHGRAQLTLAGAGELLAEDLRQAQHALGEITGAFSSDDLLGRIFSSFCIGK |
Interaction
Subunit
Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 216-379 | TrmE-type G | ||||
Sequence: GMTVVIAGRPNAGKSSLLNQLAGREAAIVTDIAGTTRDILREHIHIDGMPLHVVDTAGLRDTDDHVEKIGVERALKAIGEADRVLLVVDSTAPEASDPFALWPEFLAQRPDPAKVTLIRNKADLSGERVALEQCDDGHVTITLSAKGDDTGLQLLRDHLKGCMG |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length456
- Mass (Da)48,963
- Last updated2005-03-01 v1
- ChecksumB5E10A71C3FC5622
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X62540 EMBL· GenBank· DDBJ | CAA44418.1 EMBL· GenBank· DDBJ | Genomic DNA |