Q5S3I3 · DDMC_STEMA

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).

Catalytic activity

Cofactor

[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

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 μMdicamba
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.

TypeIDPosition(s)Description
Binding site48[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site50[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site67[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site70[2Fe-2S] cluster (UniProtKB | ChEBI)
Site153Plays a role in the stabilization of the metal coordination
Binding site159Fe cation (UniProtKB | ChEBI)
Binding site164Fe cation (UniProtKB | ChEBI)
Binding site2293,6-dichloro-2-methoxybenzoate (UniProtKB | ChEBI)
Binding site2503,6-dichloro-2-methoxybenzoate (UniProtKB | ChEBI)
Binding site2843,6-dichloro-2-methoxybenzoate (UniProtKB | ChEBI)
Binding site293Fe cation (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functionmetal ion binding
Molecular Functionmonooxygenase activity
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Biological Processcatabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dicamba O-demethylase, oxygenase component
  • EC number
  • Alternative names
    • Dicamba monooxygenase
      (DMO
      )
    • Three-component Rieske non-heme iron oxygenase system

Gene names

    • Name
      ddmC

Organism names

Accessions

  • Primary accession
    Q5S3I3

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis153Strong reduction of O-demethylase activity.
Mutagenesis156Strong reduction of O-demethylase activity.
Mutagenesis159Loss of O-demethylase activity.
Mutagenesis164Loss of O-demethylase activity.
Mutagenesis293Loss of O-demethylase activity.

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00004452552-339Dicamba O-demethylase, oxygenase component

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).

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain8-110Rieske

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    339
  • Mass (Da)
    37,299
  • Last updated
    2004-12-21 v1
  • Checksum
    7A86792D83DE4C3B
MTFVRNAWYVAALPEELSEKPLGRTILDTPLALYRQPDGVVAALLDICPHRFAPLSDGILVNGHLQCPYHGLEFDGGGQCVHNPHGNGARPASLNVRSFPVVERDALIWIWPGDPALADPGAIPDFGCRVDPAYRTVGGYGHVDCNYKLLVDNLMDLGHAQYVHRANAQTDAFDRLEREVIVGDGEIQALMKIPGGTPSVLMAKFLRGANTPVDAWNDIRWNKVSAMLNFIAVAPEGTPKEQSIHSRGTHILTPETEASCHYFFGSSRNFGIDDPEMDGVLRSWQAQALVKEDKVVVEAIERRRAYVEANGIRPAMLSCDEAAVRVSREIEKLEQLEAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY786443
EMBL· GenBank· DDBJ
AAV53699.1
EMBL· GenBank· DDBJ
Genomic DNA

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