Q5S3I3 · DDMC_STEMA
- ProteinDicamba O-demethylase, oxygenase component
- GeneddmC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids339 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the dicamba O-demethylase multicomponent enzyme system involved in the degradation of the herbicide dicamba (PubMed:15820213, PubMed:15855162, PubMed:16535584).
In vitro, catalyzes the O-demethylation of 2-methoxy-3,6-dichlorobenzoic acid (dicamba) to yield 3,6-dichlorosalicylic acid (DCSA) via an exocyclic monooxygenation (PubMed:15820213, PubMed:15855162, PubMed:16535584, PubMed:19616009).
In vitro, catalyzes the O-demethylation of 2-methoxy-3,6-dichlorobenzoic acid (dicamba) to yield 3,6-dichlorosalicylic acid (DCSA) via an exocyclic monooxygenation (PubMed:15820213, PubMed:15855162, PubMed:16535584, PubMed:19616009).
Catalytic activity
- 3,6-dichloro-2-methoxybenzoate + 2 H+ + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3,6-dichlorosalicylate + formaldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Cofactor
Note: Binds 1 [2Fe-2S] cluster per subunit.
Activity regulation
Activity enhanced by Fe2+ and Mg2+ ions.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
8 μM | dicamba |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
150 nmol/min/mg |
pH Dependence
Optimum pH is between 6.5-7.5.
Temperature Dependence
Optimum temperature is 30 degrees Celsius.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 50 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 67 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 70 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 153 | Plays a role in the stabilization of the metal coordination | ||||
Sequence: N | ||||||
Binding site | 159 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 164 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 229 | 3,6-dichloro-2-methoxybenzoate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 250 | 3,6-dichloro-2-methoxybenzoate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 284 | 3,6-dichloro-2-methoxybenzoate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 293 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | monooxygenase activity | |
Molecular Function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | |
Biological Process | catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDicamba O-demethylase, oxygenase component
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Lysobacteraceae > Stenotrophomonas > Stenotrophomonas maltophilia group
Accessions
- Primary accessionQ5S3I3
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 153 | Strong reduction of O-demethylase activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 156 | Strong reduction of O-demethylase activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 159 | Loss of O-demethylase activity. | ||||
Sequence: H → N | ||||||
Mutagenesis | 164 | Loss of O-demethylase activity. | ||||
Sequence: H → N | ||||||
Mutagenesis | 293 | Loss of O-demethylase activity. | ||||
Sequence: D → N |
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000445255 | 2-339 | Dicamba O-demethylase, oxygenase component | |||
Sequence: TFVRNAWYVAALPEELSEKPLGRTILDTPLALYRQPDGVVAALLDICPHRFAPLSDGILVNGHLQCPYHGLEFDGGGQCVHNPHGNGARPASLNVRSFPVVERDALIWIWPGDPALADPGAIPDFGCRVDPAYRTVGGYGHVDCNYKLLVDNLMDLGHAQYVHRANAQTDAFDRLEREVIVGDGEIQALMKIPGGTPSVLMAKFLRGANTPVDAWNDIRWNKVSAMLNFIAVAPEGTPKEQSIHSRGTHILTPETEASCHYFFGSSRNFGIDDPEMDGVLRSWQAQALVKEDKVVVEAIERRRAYVEANGIRPAMLSCDEAAVRVSREIEKLEQLEAA |
Interaction
Subunit
Homotrimer (PubMed:15820213, PubMed:19616009, PubMed:19616011).
The dicamba O-demethylase multicomponent enzyme system is composed of an oxygenase component (DdmC) and an electron transfer component formed by a ferredoxin reductase (DdmA) and a ferredoxin (DdmB) (PubMed:15820213, PubMed:15855162, PubMed:16535584).
In vitro, dicamba O-demethylase assays in which DdmA2 is substituted for DdmA1 demonstrate that the two enzymes possess nearly identical activities (PubMed:15855162).
The dicamba O-demethylase multicomponent enzyme system is composed of an oxygenase component (DdmC) and an electron transfer component formed by a ferredoxin reductase (DdmA) and a ferredoxin (DdmB) (PubMed:15820213, PubMed:15855162, PubMed:16535584).
In vitro, dicamba O-demethylase assays in which DdmA2 is substituted for DdmA1 demonstrate that the two enzymes possess nearly identical activities (PubMed:15855162).
Structure
Sequence
- Sequence statusComplete
- Length339
- Mass (Da)37,299
- Last updated2004-12-21 v1
- Checksum7A86792D83DE4C3B
Keywords
- Technical term