A0A5C6LQD7 · A0A5C6LQD7_9BACT

  • Protein
    Cysteine desulfurase IscS
  • Gene
    iscS
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.

Caution

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

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Cofactor biosynthesis; iron-sulfur cluster biosynthesis.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site74-75pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site154pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site182pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site202-204pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site243pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Active site329Cysteine persulfide intermediate
Binding site329[2Fe-2S] cluster (UniProtKB | ChEBI); ligand shared with IscU; via persulfide group

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functioncysteine desulfurase activity
Molecular Functionmetal ion binding
Molecular Functionpyridoxal phosphate binding
Biological Process[2Fe-2S] cluster assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cysteine desulfurase IscS
  • EC number

Gene names

    • Name
      iscS
    • ORF names
      FEF09_18685

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • YS-16
  • Taxonomic lineage
    Bacteria > Bacteroidota > Chitinophagia > Chitinophagales > Chitinophagaceae > Chitinophaga

Accessions

  • Primary accession
    A0A5C6LQD7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue205N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer. Forms a heterotetramer with IscU, interacts with other sulfur acceptors.

Family & Domains

Features

Showing features for domain, coiled coil.

Type
IDPosition(s)Description
Domain6-369Aminotransferase class V
Coiled coil256-290

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    405
  • Mass (Da)
    44,038
  • Last updated
    2019-11-13 v1
  • MD5 Checksum
    67CDDCF43857268EE9813C7E50C0BC2C
MLKLPVYLDYNATTPCDPRVVEAMLPYFSETFGNASSRNHSFGWAAEAAVDLAREQVAALIGADPKEIIFTSGATEADNLAMKGVFEMYADKGNHIITTEIEHKAVLDTCKHLEKLGAEVTYLKVNSEGLPDLKELEAAITPKTILVSIMYANNEIGVINPIKEISAIAKKHGVLMMSDISQAAGKVPVDVNRDGIDLAAFSAHKLYGTKGAGALYVRRKSPRVKVTAQMDGGGHERGMRSGTLNVPGIVAFGKACELCQQEMEAEGQRLAALRDKLENALLQLEETVVNGSKTNRLPHATNISFRYVEGEALMMGFNKNLALSSGSACTSASPEPSYVLKGLGLSDDMAHSSIRFALGRFTTEEEIDYAIQTVTDTVNKLREISPLWEMFKEGADMSSIEWSRL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VOHS01000019
EMBL· GenBank· DDBJ
TWV99081.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help