A0A140D6I5 · A0A140D6I5_9ENTR

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

Function

function

Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.

Catalytic activity

Cofactor

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

Pathway

Cofactor biosynthesis; iron-sulfur cluster biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site364Cysteine persulfide intermediate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functioncysteine desulfurase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functionselenocysteine lyase activity
Biological Processcysteine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cysteine desulfurase
  • EC number
  • Alternative names
    • Selenocysteine beta-lyase
      (SCL
      )
    • Selenocysteine lyase
      (EC:4.4.1.16
      ) . EC:4.4.1.16 (UniProtKB | ENZYME | Rhea)
    • Selenocysteine reductase

Gene names

    • Name
      sufS

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • T4-1Contig1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella

Accessions

  • Primary accession
    A0A140D6I5

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue226N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer. Interacts with SufE and the SufBCD complex composed of SufB, SufC and SufD. The interaction with SufE is required to mediate the direct transfer of the sulfur atom from the S-sulfanylcysteine.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain25-394Aminotransferase class V

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    406
  • Mass (Da)
    43,708
  • Last updated
    2016-05-11 v1
  • Checksum
    4BAFF37E450D5FF8
MTFSVERVRADFPLLGREVNGQPLVYLDSAASAQKPEAVIHAEAEFYRHGYAAVHRGIHTLSAEATTRMEQVRQRAATFLNARSAEELVFVRGTTEGINLVANSWGNANVGAGDNIIVSAMEHHANIVPWQLLCARVGAELRVIPLNPDGTLQLEAIAGLFDARTRLLAITQVSNVLGIENPVAALIALAHQHGARVLVDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYGKAALLDEMPPWEGGGSMIATVSLTQGTTWAKAPWRFEAGTPNTGGIIGLGAALEYVSALGLAQIGEYEQTLMRYALQELAKVPDLIIYGPPQRLGVIAFNLGAHHAYDVGSFLDNYGIAIRTGHHCAMPLMDFFSVPAMCRASLAMYNTTEDVDRLVAGLQRIHKLLG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KU505138
EMBL· GenBank· DDBJ
AMK07481.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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