Q9WZC1 · MIAB_THEMA
- ProteintRNA-2-methylthio-N(6)-dimethylallyladenosine synthase
- GenemiaB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids443 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i6A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms2i6A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic activity
- N6-dimethylallyladenosine37 in tRNA + [sulfur carrier]-SH + AH2 + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N6-dimethylallyladenosine37 in tRNA + [sulfur carrier]-H + 5'-deoxyadenosine + L-methionine + A + S-adenosyl-L-homocysteine + 2 H+This reaction proceeds in the forward direction.
- N6-dimethylallyladenosine37 in tRNA + [sulfur carrier]-SH + AH2 + S-adenosyl-L-methionine = 2-thio-N6-dimethylallyladenosine37 in tRNA + [sulfur carrier]-H + 5'-deoxyadenosine + L-methionine + A + H+This reaction proceeds in the forward direction.
- 2-thio-N6-dimethylallyladenosine37 in tRNA + S-adenosyl-L-methionine = 2-methylsulfanyl-N6-dimethylallyladenosine37 in tRNA + S-adenosyl-L-homocysteine + H+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 10 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 46 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 79 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 150 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 154 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 157 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | N6-isopentenyladenosine methylthiotransferase activity | |
Biological Process | tRNA methylthiolation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nametRNA-2-methylthio-N(6)-dimethylallyladenosine synthase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermotogota > Thermotogae > Thermotogales > Thermotogaceae > Thermotoga
Accessions
- Primary accessionQ9WZC1
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 10 | Loss of activity. | |||
Mutagenesis | 150 | Decreased iron content and loss of activity; when associated with A-154 and A-157. | |||
Mutagenesis | 154 | Decreased iron content and loss of activity; when associated with A-150 and A-157. | |||
Mutagenesis | 157 | Decreased iron content and loss of activity; when associated with A-150 and A-154. | |||
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000359590 | 1-443 | tRNA-2-methylthio-N6-dimethylallyladenosine synthase | ||
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 1-114 | MTTase N-terminal | |||
Domain | 136-367 | Radical SAM core | |||
Domain | 370-431 | TRAM | |||
Sequence similarities
Belongs to the methylthiotransferase family. MiaB subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length443
- Mass (Da)50,742
- Last updated1999-11-01 v1
- Checksum2C738B79667C9895
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000512 EMBL· GenBank· DDBJ | AAD35737.1 EMBL· GenBank· DDBJ | Genomic DNA |