Q727N0 · ISLB_NITV2

Function

function

Involved in an anaerobic respiration pathway that converts the sulfonate isethionate (2-hydroxyethanesulfonate) to ammonia, acetate and sulfide. Catalyzes activation of the isethionate sulfite-lyase IseG under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).

Catalytic activity

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 3 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.

Pathway

Organosulfur degradation; alkanesulfonate degradation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site36[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site40[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site42-44S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site43[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site62[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site68[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site71[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site75[4Fe-4S] cluster 3 (UniProtKB | ChEBI)
Binding site95[4Fe-4S] cluster 3 (UniProtKB | ChEBI)
Binding site98[4Fe-4S] cluster 3 (UniProtKB | ChEBI)
Binding site102[4Fe-4S] cluster 3 (UniProtKB | ChEBI)
Binding site106[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site146S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site195-197S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site268S-adenosyl-L-methionine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity
Biological Processalkanesulfonate catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Isethionate sulfite-lyase activating enzyme
  • EC number
  • Alternative names
    • GRE activase IseH
    • Glycyl-radical enzyme activating enzyme IseH

Gene names

    • Name
      iseH
    • Ordered locus names
      DVU_2825

Organism names

Accessions

  • Primary accession
    Q727N0

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004509481-307Isethionate sulfite-lyase activating enzyme

Proteomic databases

Interaction

Subunit

Monomer.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q727N0DVU_2677 Q728C62EBI-10066541, EBI-10066547

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain22-307Radical SAM core
Domain53-854Fe-4S ferredoxin-type 1
Domain86-1174Fe-4S ferredoxin-type 2

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    307
  • Mass (Da)
    33,738
  • Last updated
    2004-07-05 v1
  • Checksum
    017AA3D4880B0695
MSSIADRKTTGITFNIQKYSVHDGPGIRTVVFLKGCPLKCRWCSNPESQRKSVELAYNTGRCLTLAKCVRCVEICTAGAISRAEDDTISIDRALCNDCEQLCSGACPSNALITYGAHKTVDEVLRAVEQDSLFYARSGGGMTISGGEPFAQPAFTLALLREARRRRVHTAVETCGYASWDDMAAALPFLNYVLYDIKNLDDARHKEATGVSNQRIVENLRALRAEFPGIPVLVRTPVIPGFNDNEADIAAIAALTRELGVSYQLLPYHRLGTQKYHFLDREAPMGEVTLDAETMRRLEAVVAQTADS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE017285
EMBL· GenBank· DDBJ
AAS97297.1
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.
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