A0A1V2KPG9 · A0A1V2KPG9_9ACTN
- ProteinMycothiol acetyltransferase
- GenemshD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids340 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic activity
- 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = mycothiol + CoA + H+
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 36 | 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside (UniProtKB | ChEBI) | |||
Binding site | 79-81 | acetyl-CoA 1 (UniProtKB | ChEBI) | |||
Binding site | 206 | 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside (UniProtKB | ChEBI) | |||
Binding site | 245 | 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside (UniProtKB | ChEBI) | |||
Binding site | 266 | 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside (UniProtKB | ChEBI) | |||
Binding site | 270-272 | acetyl-CoA 2 (UniProtKB | ChEBI) | |||
Binding site | 277-283 | acetyl-CoA 2 (UniProtKB | ChEBI) | |||
Binding site | 304 | 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside (UniProtKB | ChEBI) | |||
Binding site | 309-314 | acetyl-CoA 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | mycothiol synthase activity | |
Molecular Function | peptide-alanine-alpha-N-acetyltransferase activity | |
Biological Process | mycothiol biosynthetic process | |
Biological Process | N-terminal peptidyl-alanine acetylation |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMycothiol acetyltransferase
- EC number
- Short namesMSH acetyltransferase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Frankiales > Frankiaceae > Frankia
Accessions
- Primary accessionA0A1V2KPG9
Proteomes
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 5-148 | N-acetyltransferase | |||
Compositional bias | 146-165 | Polar residues | |||
Region | 146-175 | Disordered | |||
Domain | 179-340 | N-acetyltransferase | |||
Sequence similarities
Belongs to the acetyltransferase family. MshD subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length340
- Mass (Da)35,449
- Last updated2017-06-07 v1
- MD5 Checksum0DC75E9970B6EA6CFC3018E111E19816
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 146-165 | Polar residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MOWP01000017 EMBL· GenBank· DDBJ | ONH59618.1 EMBL· GenBank· DDBJ | Genomic DNA |