A0A9X3IAU8 · A0A9X3IAU8_9SPHI

  • 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 site73-74pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site153pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site181pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site201-203pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site242pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Active site327Cysteine persulfide intermediate
Binding site327[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
      OQZ29_16685

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 19486
  • Taxonomic lineage
    Bacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Pedobacter

Accessions

  • Primary accession
    A0A9X3IAU8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue204N6-(pyridoxal phosphate)lysine

Interaction

Subunit

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

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-367Aminotransferase class V

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    403
  • Mass (Da)
    44,119
  • Last updated
    2023-11-08 v1
  • Checksum
    3E9A216ADF250C07
MKQPIYLDNNATTPLDPRVLEAMLPYFTEKFGNAASRNHAFGWVAEEGVDYAREQVAKLIGCTEKEVIFTSGATEADNLAIKGVFEMYKDKGNHIITAVTEHKAVLDTCKHLEKNGARVTYLGVKEDGLIDLAELEAAMTPETILVSIMYGNNEIGVIQPVKEISAIAHKHGALFMTDATQAVGKIPVDVNADGIDLMAFSAHKMYGPKGVGALYVRRKNPRVKVTSQMDGGGHERGMRSGTLNVPGIVGLGKACELCRLEMESETIRLSALRDKLETTLNKMEESYVNGNTQHRLPHVANISFKYVEGEGLMMAMSDLAVSSGSACTSASLEPSYVLKSLGLSDDLAHSSIRYGLGRFTTEEEIDQAIAVTQKAVNHLRELSPLWEMFKEGIDLSKIEWAEH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAPJUH010000005
EMBL· GenBank· DDBJ
MCX3266399.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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