Q312S3 · ISLB_OLEA2
- ProteinIsethionate sulfite-lyase activating enzyme
- GeneislB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids309 (go to sequence)
- Protein existenceEvidence at transcript 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 IslA 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 > Oleidesulfovibrio
Accessions
- Primary accessionQ312S3
Proteomes
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene lose the ability to grow with isethionate as the terminal electron acceptor.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450946 | 1-309 | Isethionate sulfite-lyase activating enzyme | |||
Sequence: MSSFEDKKTTGITFNIQKYSVHDGPGIRTVVFLKGCPLRCRWCSNPESQRRRIELAYNTGRCLTLTKCVRCVEVCTMNAITRADDDTISIDRALCEECGMFCAEACPSKALITYGTTRTVDEVLNVVEQDSVFYARSGGGITLSGGEPFAQPAFALALLREARRRHIHTAVETCGYASWSDMEPALEYVKFVHYDIKSLDDEKHRSATGVSNVRIIENLRNIRSRFPALKVVVRTPVIPGFNDTEEDIRAIARLTAELEVEYQLLPYHRLGTQKYTFLDRQAPMGEVVLDEQVMTALNAVVAAEHATDG |
Expression
Induction
Highly up-regulated in the presence of isethionate.
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-309 | Radical SAM core | ||||
Sequence: HDGPGIRTVVFLKGCPLRCRWCSNPESQRRRIELAYNTGRCLTLTKCVRCVEVCTMNAITRADDDTISIDRALCEECGMFCAEACPSKALITYGTTRTVDEVLNVVEQDSVFYARSGGGITLSGGEPFAQPAFALALLREARRRHIHTAVETCGYASWSDMEPALEYVKFVHYDIKSLDDEKHRSATGVSNVRIIENLRNIRSRFPALKVVVRTPVIPGFNDTEEDIRAIARLTAELEVEYQLLPYHRLGTQKYTFLDRQAPMGEVVLDEQVMTALNAVVAAEHATDG | ||||||
Domain | 53-85 | 4Fe-4S ferredoxin-type 1 | ||||
Sequence: IELAYNTGRCLTLTKCVRCVEVCTMNAITRADD | ||||||
Domain | 86-117 | 4Fe-4S ferredoxin-type 2 | ||||
Sequence: DTISIDRALCEECGMFCAEACPSKALITYGTT |
Sequence similarities
Belongs to the organic radical-activating enzymes family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length309
- Mass (Da)34,567
- Last updated2005-12-06 v1
- Checksum8FE38F4981B65817
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000112 EMBL· GenBank· DDBJ | ABB38073.1 EMBL· GenBank· DDBJ | Genomic DNA |