DDMA1_STEMA
ID DDMA1_STEMA Reviewed; 408 AA.
AC Q5S3I2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Dicamba O-demethylase 1, ferredoxin reductase component {ECO:0000303|PubMed:16535584};
DE AltName: Full=Ferredoxin--NAD(+) reductase {ECO:0000303|PubMed:16535584};
DE EC=1.18.1.3 {ECO:0000305|PubMed:15820213, ECO:0000305|PubMed:15855162, ECO:0000305|PubMed:16535584};
GN Name=ddmA1 {ECO:0000303|PubMed:15855162};
OS Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS maltophilia).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=40324 {ECO:0000312|EMBL:AAV53700.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RC STRAIN=DI-6 {ECO:0000312|EMBL:AAV53700.1};
RX PubMed=15855162; DOI=10.1074/jbc.m500597200;
RA Herman P.L., Behrens M., Chakraborty S., Chrastil B.M., Barycki J.,
RA Weeks D.P.;
RT "A three-component dicamba O-demethylase from Pseudomonas maltophilia,
RT strain DI-6: gene isolation, characterization, and heterologous
RT expression.";
RL J. Biol. Chem. 280:24759-24767(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=DI-6;
RX PubMed=15820213; DOI=10.1016/j.abb.2005.02.024;
RA Chakraborty S., Behrens M., Herman P.L., Arendsen A.F., Hagen W.R.,
RA Carlson D.L., Wang X.Z., Weeks D.P.;
RT "A three-component dicamba O-demethylase from Pseudomonas maltophilia,
RT strain DI-6: purification and characterization.";
RL Arch. Biochem. Biophys. 437:20-28(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=DI-6;
RX PubMed=16535584; DOI=10.1128/aem.63.4.1623-1626.1997;
RA Wang X., Li B., Herman P.L., Weeks D.P.;
RT "A three-component enzyme system catalyzes the O-demethylation of the
RT herbicide dicamba in Pseudomonas maltophilia DI-6.";
RL Appl. Environ. Microbiol. 63:1623-1626(1997).
CC -!- FUNCTION: Component of the dicamba O-demethylase multicomponent enzyme
CC system involved in the degradation of the herbicide dicamba
CC (PubMed:15855162, PubMed:15820213, PubMed:16535584). In vitro,
CC catalyzes the transfers of electrons from ferredoxin (DdmB) to NADH
CC (PubMed:15855162, PubMed:15820213, PubMed:16535584). Both NADH and
CC NADPH support enzyme activity, with NADH being markedly more effective
CC than NADPH (PubMed:15820213, PubMed:16535584).
CC {ECO:0000269|PubMed:15820213, ECO:0000269|PubMed:15855162,
CC ECO:0000269|PubMed:16535584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.3;
CC Evidence={ECO:0000305|PubMed:15820213, ECO:0000305|PubMed:15855162,
CC ECO:0000305|PubMed:16535584};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:15820213};
CC -!- SUBUNIT: Monomer (PubMed:15820213). The dicamba O-demethylase
CC multicomponent enzyme system is composed of an oxygenase component
CC (DdmC) and an electron transfer component formed by a ferredoxin
CC reductase (DdmA1) and a ferredoxin (DdmB) (PubMed:15855162,
CC PubMed:15820213, PubMed:16535584). In vitro, dicamba O-demethylase
CC assays in which DdmA2 is substituted for DdmA1 demonstrate that the two
CC enzymes possess nearly identical activities (PubMed:15855162).
CC {ECO:0000269|PubMed:15820213, ECO:0000269|PubMed:15855162,
CC ECO:0000269|PubMed:16535584}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AY786444; AAV53700.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5S3I2; -.
DR SMR; Q5S3I2; -.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15820213"
FT CHAIN 2..408
FT /note="Dicamba O-demethylase 1, ferredoxin reductase
FT component"
FT /id="PRO_0000445256"
FT BINDING 14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
SQ SEQUENCE 408 AA; 43666 MW; 6356773DC1439824 CRC64;
MSKADVVIVG AGHGGAQCAI ALRQNGFEGT ITVIGREPEY PYERPPLSKE YFAREKTFDR
LYIRPPTFWA EKNIEFKLGT EVTKVDPKAH ELTLSNGESY GYGKLVWATG GDPRRLSCQG
ADLTGIHAVR TREDCDTLMA EVDAGTKNIV VIGGGYIGLE AAAVLSKMGL KVTLLEALPR
VLARVAGEDL STFYQKEHVD HGVDLRTEVM VDSLVGENGK VTGVQLAGGE VIPAEGVIVG
IGIVPAVGPL IAAGAAGANG VDVDEYCRTS LPDIYAIGDC AAFACDYAGG NVMRVESVQN
ANDMGTCVAK AICGDEKPYK AFPWFWSNQY DLKLQTAGIN LGFDKTVIRG NPEERSFSVV
YLKDGRVVAL DCVNMVKDYV QGRKLVEAGA TPDLEALADA GKPLKELL
