F0M1A9 · F0M1A9_PSEPM
- ProteinL-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
- GenemshC
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids425 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.
Catalytic activity
- 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + ATP + L-cysteine = 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + AMP + diphosphate + H+
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 43 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 43-46 | L-cysteinyl-5'-AMP (UniProtKB | ChEBI) | ||||
Sequence: CGIT | ||||||
Binding site | 58 | L-cysteinyl-5'-AMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 81-83 | L-cysteinyl-5'-AMP (UniProtKB | ChEBI) | ||||
Sequence: NVT | ||||||
Binding site | 240 | L-cysteinyl-5'-AMP (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 244 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 262-264 | L-cysteinyl-5'-AMP (UniProtKB | ChEBI) | ||||
Sequence: GSD | ||||||
Binding site | 269 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 295 | L-cysteinyl-5'-AMP (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | aminoacyl-tRNA ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | cysteine-glucosaminylinositol ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | mycothiol biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
- EC number
- Short namesL-Cys:GlcN-Ins ligase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Pseudarthrobacter
Accessions
- Primary accessionF0M1A9
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-349 | tRNA synthetases class I catalytic | ||||
Sequence: QENHPSMYVCGITPYDATHMGHASSYVAFDLLNRAWRDAGQEVAYVQNVTDVDDPLLERATATGVDWRDLAAGQIELFQTDMEALNVLPPDHYVGAVESIGLIVPEVERLVSLGLAYKVDGTNGEPDGDVYYDVEAAGKQSVAPDAWTLGCISGLNESEMLELFAERGGDPGRAGKRQALDPLLWRVEREGEPSWPGGSLGPGRPGWHIECTVIAQKYLPQPFTVQGGGSDLIFPHHEMGAGHAYSLAGVPLARHYAHAGMVGLDGEKMSKSKGNLVLVSKLRAAGEDPAAIRLGILAHHYRSDWSWTDHGFEDAK | ||||||
Motif | 45-55 | 'HIGH' region | ||||
Sequence: ITPYDATHMGH | ||||||
Motif | 199-204 | 'ERGGDP' region | ||||
Sequence: ERGGDP | ||||||
Motif | 301-305 | 'KMSKS' region | ||||
Sequence: KMSKS |
Sequence similarities
Belongs to the class-I aminoacyl-tRNA synthetase family. MshC subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length425
- Mass (Da)45,338
- Last updated2011-05-03 v1
- ChecksumFCA0EE1EF1513148
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002379 EMBL· GenBank· DDBJ | ADX73048.1 EMBL· GenBank· DDBJ | Genomic DNA |