ID   DDMA2_STEMA             Reviewed;         409 AA.
AC   Q5S3I1;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Dicamba O-demethylase 2, ferredoxin reductase component {ECO:0000303|PubMed:15855162};
DE   AltName: Full=Ferredoxin--NAD(+) reductase {ECO:0000303|PubMed:15855162};
DE            EC=1.18.1.3 {ECO:0000305|PubMed:15855162};
GN   Name=ddmA2 {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:AAV53701.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBUNIT.
RC   STRAIN=DI-6 {ECO:0000312|EMBL:AAV53701.1};
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).
CC   -!- FUNCTION: Component of the dicamba O-demethylase multicomponent enzyme
CC       system involved in the degradation of the herbicide dicamba
CC       (PubMed:15855162). In vitro, catalyzes the transfers of electrons from
CC       ferredoxin (DdmB) to NADH (PubMed:15855162). Both NADH and NADPH
CC       support enzyme activity, with NADH being markedly more effective than
CC       NADPH (By similarity). {ECO:0000250|UniProtKB:Q5S3I2,
CC       ECO:0000269|PubMed:15855162}.
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:15855162};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q5S3I2};
CC   -!- SUBUNIT: Monomer (By similarity). 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). In vitro
CC       dicamba O-demethylase assays in which DdmA2 is substituted for DdmA1
CC       demonstrate that the two enzymes possess nearly identical activities
CC       (PubMed:15855162). {ECO:0000250|UniProtKB:Q5S3I2,
CC       ECO:0000269|PubMed:15855162}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; AY786445; AAV53701.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5S3I1; -.
DR   SMR; Q5S3I1; -.
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   FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..409
FT                   /note="Dicamba O-demethylase 2, ferredoxin reductase
FT                   component"
FT                   /id="PRO_0000445257"
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   409 AA;  43927 MW;  50A6F1EDE8B3FCC1 CRC64;
     MQRADVVIVG AGHGGAQCAI ALRQNGFEGT ITVIGREPEY PYERPPLSKE YFAREKTFDR
     LYIRPPTFWA EKNIEFKLGT EVTKVDPKAH ELTLSNGESY GYGKLVWATG GDPRRLSCQG
     ADLTGIHAVR TREDCDTLMA EVDAGTKNIV VIGGGYIGLE AAAVLSKMGL KVTLLEALPR
     VLARVAGEDL STFYQKEHVD HGVDLRTEVM VDSLVGENGK VTGVQLAGGE VIPAEGVIVG
     IGIVPAIGPL IAAGAAGANG VDVDEYCRTS LPDIYAIGDC AAFACDYAGG NVMRVESVQN
     ANDMGTCVAK AICGDEKPYK AFPWFWSNQY DLKLQTAGIN LGFDKTVIRG NPEERSFSVV
     YLKDGRVVAL DCVNMVKDYV QGRKLVEAGA TPDLEALADA GKPLKELQY