Q312S2 · ISLA_OLEA2
- ProteinIsethionate sulfite-lyase
- GeneislA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids829 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Involved in an anaerobic respiration pathway that converts the sulfonate isethionate (2-hydroxyethanesulfonate) to ammonia, acetate and sulfide. Catalyzes the radical-mediated C-S bond cleavage of isethionate (2-hydroxyethanesulfonate) to form sulfite and acetaldehyde.
Catalytic activity
- 2-hydroxyethane-1-sulfonate = acetaldehyde + H+ + sulfiteThis reaction proceeds in the forward direction.
Pathway
Organosulfur degradation; alkanesulfonate degradation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 188 | 2-hydroxyethane-1-sulfonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 192 | 2-hydroxyethane-1-sulfonate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 467 | Cysteine radical intermediate | ||||
Sequence: C | ||||||
Binding site | 467-469 | 2-hydroxyethane-1-sulfonate (UniProtKB | ChEBI) | ||||
Sequence: CTE | ||||||
Active site | 469 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 677 | 2-hydroxyethane-1-sulfonate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | lyase activity | |
Biological Process | alkanesulfonate catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIsethionate sulfite-lyase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Oleidesulfovibrio
Accessions
- Primary accessionQ312S2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000450942 | 1-829 | Isethionate sulfite-lyase | |||
Sequence: MQCCTTPLSPHEQRLQDKIAGKEDSFRKSHERVFNILDSFDGKRPRIDVERAKLFTDSMKETEGQPLVLRWAKAMKHVAEHITVYIDDDQLICGRGGCPGRYGVLYPELDGDFLDLAIEDLPNRTESPFTITEADARVVVEEIAPYWKGKTYHEDLNLALPSDVHKLTYDDPQGLKSRFIVNETSSFRSSIQWVHDYEKVLKRGFRGLKEEAQEKIAGLDPLSPRDNVEKRPFLEAIVIVCDAIILWANRHAKLAADMAAAETNPVRKAELETMAEICAWVPENPARNFYEAVQAQWFTQMFSRLEQKTGTIVSNGRMDQYFWPFYRKDIEEGRITEESALELLECMWVGMAQYVDLYISPAGGAFNEGYAHWEAVTIGGQTPQGLDATNDLTYLFLKSKREFPLHYPDLAARIHSRSPERYLHDVAETIKFGSGFPKLINDEEIVPLYVSKGASFEEALDYAVSGCTEARMPNRDTYTSGGAYINFAAALEMVLYNGRMLKYGENELGLETGDPTRFETWEEFWNAYVLQHEHFLRAAFIQQHIINNVRARHFAQPMGSALHDLCMKHCLDLHTPQIPEGINLGYFEYMGFGTVVDSLAAIKKLVFEDKKLTMQEVIEALKCNFEGKEDVQQMLKSAPCYGNNDEYADSIAREIDAISVKYGRRYSPELGMHNDVRYVPFTSHVPFGKVVSATPNGRLAWTPLSDGSSASHGADVNGPTAVLQSNFSSKNYGYRDRAARMLNIKFTPKCVEGDEGTEKLVSFIRTFCDLKLWHVQFNVINRDTLIAAQKDPEKYRSLIVRIAGYSAYFVDLSPDLQNDLIARTQHDAM | ||||||
Modified residue | 804 | Glycine radical | ||||
Sequence: G |
Post-translational modification
Requires the activating protein IslB to generate the key active site glycyl radical on Gly-804 that is involved in catalysis.
Keywords
- PTM
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 | 31-699 | PFL | ||||
Sequence: ERVFNILDSFDGKRPRIDVERAKLFTDSMKETEGQPLVLRWAKAMKHVAEHITVYIDDDQLICGRGGCPGRYGVLYPELDGDFLDLAIEDLPNRTESPFTITEADARVVVEEIAPYWKGKTYHEDLNLALPSDVHKLTYDDPQGLKSRFIVNETSSFRSSIQWVHDYEKVLKRGFRGLKEEAQEKIAGLDPLSPRDNVEKRPFLEAIVIVCDAIILWANRHAKLAADMAAAETNPVRKAELETMAEICAWVPENPARNFYEAVQAQWFTQMFSRLEQKTGTIVSNGRMDQYFWPFYRKDIEEGRITEESALELLECMWVGMAQYVDLYISPAGGAFNEGYAHWEAVTIGGQTPQGLDATNDLTYLFLKSKREFPLHYPDLAARIHSRSPERYLHDVAETIKFGSGFPKLINDEEIVPLYVSKGASFEEALDYAVSGCTEARMPNRDTYTSGGAYINFAAALEMVLYNGRMLKYGENELGLETGDPTRFETWEEFWNAYVLQHEHFLRAAFIQQHIINNVRARHFAQPMGSALHDLCMKHCLDLHTPQIPEGINLGYFEYMGFGTVVDSLAAIKKLVFEDKKLTMQEVIEALKCNFEGKEDVQQMLKSAPCYGNNDEYADSIAREIDAISVKYGRRYSPELGMHNDVRYVPFTSHVPFGKVVSATPNGRL | ||||||
Domain | 706-829 | Glycine radical | ||||
Sequence: DGSSASHGADVNGPTAVLQSNFSSKNYGYRDRAARMLNIKFTPKCVEGDEGTEKLVSFIRTFCDLKLWHVQFNVINRDTLIAAQKDPEKYRSLIVRIAGYSAYFVDLSPDLQNDLIARTQHDAM |
Sequence similarities
Belongs to the glycyl radical enzyme (GRE) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length829
- Mass (Da)94,135
- Last updated2005-12-06 v1
- Checksum3259CAE3A49AE8BB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000112 EMBL· GenBank· DDBJ | ABB38074.1 EMBL· GenBank· DDBJ | Genomic DNA |