Q5LW89 · DDDW_RUEPO
- ProteinDimethylsulfoniopropionate lyase DddW
- GenedddW
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids152 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Able to cleave dimethylsulfoniopropionate (DMSP), releasing dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere.
Catalytic activity
- S,S-dimethyl-beta-propiothetin = acrylate + dimethyl sulfide + H+
Cofactor
Note: Binds 1 Fe2+ ion per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
8.68 μM | dimethylsulfoniopropionate | in the presence of Fe2+ | ||||
4.5 μM | dimethylsulfoniopropionate | in the presence of Mn2+ |
kcat is 18.25 sec-1 with dimethylsulfoniopropionate (in the presence of Fe2+).
kcat is 17.33 sec-1 with dimethylsulfoniopropionate (in the presence of Mn2+).
kcat is 17.33 sec-1 with dimethylsulfoniopropionate (in the presence of Mn2+).
pH Dependence
Optimum pH is 8.0.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | dimethylpropiothetin dethiomethylase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDimethylsulfoniopropionate lyase DddW
- EC number
- Short namesDMSP lyase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Ruegeria
Accessions
- Primary accessionQ5LW89
Proteomes
Phenotypes & Variants
Disruption phenotype
Decreased production of dimethyl sulfide (DMS).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 81 | Decreased iron binding and enzyme activity toward DMSP. | ||||
Sequence: H → A | ||||||
Mutagenesis | 83 | Decreased iron binding and enzyme activity toward DMSP. | ||||
Sequence: H → A | ||||||
Mutagenesis | 87 | Decreased iron binding and enzyme activity toward DMSP. | ||||
Sequence: E → A | ||||||
Mutagenesis | 121 | Decreased iron binding and enzyme activity toward DMSP. | ||||
Sequence: H → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000433900 | 1-152 | Dimethylsulfoniopropionate lyase DddW | |||
Sequence: MTAMLDSFATDLTAATSLHQPGNLPHPPHAIDAENVPLSGGTDPTYGEVRWRTLINGTEAAPRDMVLGIAEFGPGHQLRPHRHTPPEFYLGLEGSGIVTIDGVPHEIRAGVALYIPGDAEHGTVAGPEGLRFAYGFASASFEAIEYRFTASA |
Proteomic databases
Expression
Induction
Up-regulated by pre-growth of cells with dimethylsulfoniopropionate (DMSP).
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 69-124 | Cupin type-2 | ||||
Sequence: IAEFGPGHQLRPHRHTPPEFYLGLEGSGIVTIDGVPHEIRAGVALYIPGDAEHGTV |
Sequence similarities
Belongs to the non-heme iron-dependent dioxygenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length152
- Mass (Da)16,132
- Last updated2005-02-01 v1
- Checksum90EF8584AEFCA325
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000031 EMBL· GenBank· DDBJ | AAV93771.1 EMBL· GenBank· DDBJ | Genomic DNA |