A0A2T5NLG1 · A0A2T5NLG1_9NEIS
- ProteinCysteine desulfurase IscS
- GeneiscS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids405 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
Catalytic activity
- [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Cofactor
Pathway
Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 76-77 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 156 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 184 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 204-206 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 244 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Active site | 329 | Cysteine persulfide intermediate | |||
Binding site | 329 | [2Fe-2S] cluster (UniProtKB | ChEBI); ligand shared with IscU; via persulfide group | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | cysteine desulfurase activity | |
Molecular Function | metal ion binding | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | [2Fe-2S] cluster assembly |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCysteine desulfurase IscS
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Neisseriales > Chromobacteriaceae > Chromobacterium
Accessions
- Primary accessionA0A2T5NLG1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 207 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer. Forms a heterotetramer with IscU, interacts with other sulfur acceptors.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 8-368 | Aminotransferase class V | |||
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length405
- Mass (Da)45,387
- Last updated2018-07-18 v1
- MD5 ChecksumA4A379545AADFDE0BE24F9D87E2BEF76
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QARX01000001 EMBL· GenBank· DDBJ | PTU66313.1 EMBL· GenBank· DDBJ | Genomic DNA |