B1LNI6 · ISCS_ECOSM

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 and selenium atoms from cysteine and selenocysteine 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. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate.

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.

TypeIDPosition(s)Description
Binding site75-76pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site155pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site183pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site203-205pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site243pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Active site328Cysteine persulfide intermediate
Binding site328[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
    • Ordered locus names
      EcSMS35_2683

Organism names

Accessions

  • Primary accession
    B1LNI6

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_10001196281-404Cysteine desulfurase IscS
Modified residue206N6-(pyridoxal phosphate)lysine

Interaction

Subunit

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

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    404
  • Mass (Da)
    45,090
  • Last updated
    2008-04-29 v1
  • Checksum
    1E4F2E6F9CD266B0
MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIEWAHH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000970
EMBL· GenBank· DDBJ
ACB18360.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp