A0A7W9IBW1 · A0A7W9IBW1_9ACTN

  • Protein
    L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
  • Gene
    mshC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site43Zn2+ (UniProtKB | ChEBI)
Binding site43-46L-cysteinyl-5'-AMP (UniProtKB | ChEBI)
Binding site58L-cysteinyl-5'-AMP (UniProtKB | ChEBI)
Binding site81-83L-cysteinyl-5'-AMP (UniProtKB | ChEBI)
Binding site223L-cysteinyl-5'-AMP (UniProtKB | ChEBI)
Binding site227Zn2+ (UniProtKB | ChEBI)
Binding site245-247L-cysteinyl-5'-AMP (UniProtKB | ChEBI)
Binding site252Zn2+ (UniProtKB | ChEBI)
Binding site279L-cysteinyl-5'-AMP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functioncysteine-glucosaminylinositol ligase activity
Molecular Functioncysteine-tRNA ligase activity
Molecular Functionzinc ion binding
Biological Processcysteinyl-tRNA aminoacylation
Biological Processmycothiol biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
  • EC number
  • Short names
    L-Cys:GlcN-Ins ligase
  • Alternative names
    • Mycothiol ligase
      (MSH ligase
      )

Gene names

    • Name
      mshC
    • ORF names
      F4562_000929

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 46887
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Streptosporangiales > Streptosporangiaceae > Streptosporangium

Accessions

  • Primary accession
    A0A7W9IBW1

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, domain, motif.

TypeIDPosition(s)Description
Region1-21Disordered
Domain38-331tRNA synthetases class I catalytic
Motif45-55'HIGH' region
Motif183-188'ERGGDP' region
Motif285-289'KMSKS' region

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. MshC subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    407
  • Mass (Da)
    44,225
  • Last updated
    2021-06-02 v1
  • Checksum
    2A3CF0B47BF9D162
MRSWSAPKVPRLPGTGAPPRLYDTAAREVAPTRPGPTARMYVCGITPYDATHLGHANTYLAFDLVNRAWRDAGHEVHFTQNATDVDDPLLKRAEETGVDWQELAEREIELFRTDMEALRIIPPREYVGVTEAIDQVAALVVLLRDKGATYDLDGDVYFDVAAAPKFGAVSGYSEEQMIALSGERGGDPDRPGKKHPLDWLLWRAERPGEPSWASPLGRGRPGWHIECTAIALANLSSGFDVAGGGSDLIFPHHECGAHEGHVACGEWPFAKAYVHAGMVALDGEKMSKSKGNLVFVSRLRRQSDPMAIRLALLAHHYRSDWEWTPDQLASAEVRLARWRSAVGLGIGPDAAGVLERVRDRIAADLDTPAALAAVDEWAERALSEGGSDPGAPTLVKDVVDALLGVAL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACHMP010000001
EMBL· GenBank· DDBJ
MBB5817867.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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