A0A140D6I5 · A0A140D6I5_9ENTR
- ProteinCysteine desulfurase
- GenesufS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids406 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.
Catalytic activity
- AH2 + L-selenocysteine = A + H+ + hydrogenselenide + L-alanine
Cofactor
Pathway
Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 364 | Cysteine persulfide intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | cysteine desulfurase activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | selenocysteine lyase activity | |
Biological Process | cysteine metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCysteine desulfurase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella
Accessions
- Primary accessionA0A140D6I5
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 226 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer. Interacts with SufE and the SufBCD complex composed of SufB, SufC and SufD. The interaction with SufE is required to mediate the direct transfer of the sulfur atom from the S-sulfanylcysteine.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-394 | Aminotransferase class V | ||||
Sequence: VYLDSAASAQKPEAVIHAEAEFYRHGYAAVHRGIHTLSAEATTRMEQVRQRAATFLNARSAEELVFVRGTTEGINLVANSWGNANVGAGDNIIVSAMEHHANIVPWQLLCARVGAELRVIPLNPDGTLQLEAIAGLFDARTRLLAITQVSNVLGIENPVAALIALAHQHGARVLVDGAQAVMHHAVDVQALDCDFYVFSGHKLYGPTGIGVLYGKAALLDEMPPWEGGGSMIATVSLTQGTTWAKAPWRFEAGTPNTGGIIGLGAALEYVSALGLAQIGEYEQTLMRYALQELAKVPDLIIYGPPQRLGVIAFNLGAHHAYDVGSFLDNYGIAIRTGHHCAMPLMDFFSVPAMCRASLAMYNTTEDVDRL |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length406
- Mass (Da)43,708
- Last updated2016-05-11 v1
- Checksum4BAFF37E450D5FF8