Q727N0 · ISLB_NITV2
- ProteinIsethionate sulfite-lyase activating enzyme
- GeneiseH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids307 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
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
- glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H+ + L-methionine + semiquinone [flavodoxin]This reaction proceeds in the forward direction.
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 36 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 40 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 42-44 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: WCS | ||||||
Binding site | 43 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 62 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 68 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 71 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 75 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 95 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 98 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 102 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 106 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 146 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 195-197 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DIK | ||||||
Binding site | 268 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | alkanesulfonate catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIsethionate sulfite-lyase activating enzyme
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Nitratidesulfovibrio
Accessions
- Primary accessionQ727N0
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450948 | 1-307 | Isethionate sulfite-lyase activating enzyme | |||
Sequence: MSSIADRKTTGITFNIQKYSVHDGPGIRTVVFLKGCPLKCRWCSNPESQRKSVELAYNTGRCLTLAKCVRCVEICTAGAISRAEDDTISIDRALCNDCEQLCSGACPSNALITYGAHKTVDEVLRAVEQDSLFYARSGGGMTISGGEPFAQPAFTLALLREARRRRVHTAVETCGYASWDDMAAALPFLNYVLYDIKNLDDARHKEATGVSNQRIVENLRALRAEFPGIPVLVRTPVIPGFNDNEADIAAIAALTRELGVSYQLLPYHRLGTQKYHFLDREAPMGEVTLDAETMRRLEAVVAQTADS |
Proteomic databases
Interaction
Subunit
Monomer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q727N0 | DVU_2677 Q728C6 | 2 | EBI-10066541, EBI-10066547 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-307 | Radical SAM core | ||||
Sequence: HDGPGIRTVVFLKGCPLKCRWCSNPESQRKSVELAYNTGRCLTLAKCVRCVEICTAGAISRAEDDTISIDRALCNDCEQLCSGACPSNALITYGAHKTVDEVLRAVEQDSLFYARSGGGMTISGGEPFAQPAFTLALLREARRRRVHTAVETCGYASWDDMAAALPFLNYVLYDIKNLDDARHKEATGVSNQRIVENLRALRAEFPGIPVLVRTPVIPGFNDNEADIAAIAALTRELGVSYQLLPYHRLGTQKYHFLDREAPMGEVTLDAETMRRLEAVVAQTADS | ||||||
Domain | 53-85 | 4Fe-4S ferredoxin-type 1 | ||||
Sequence: VELAYNTGRCLTLAKCVRCVEICTAGAISRAED | ||||||
Domain | 86-117 | 4Fe-4S ferredoxin-type 2 | ||||
Sequence: DTISIDRALCNDCEQLCSGACPSNALITYGAH |
Sequence similarities
Belongs to the organic radical-activating enzymes family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length307
- Mass (Da)33,738
- Last updated2004-07-05 v1
- Checksum017AA3D4880B0695
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE017285 EMBL· GenBank· DDBJ | AAS97297.1 EMBL· GenBank· DDBJ | Genomic DNA |