ID   MDAB_ECOL6              Reviewed;         193 AA.
AC   P0AEY6; P40717;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=NADPH:quinone oxidoreductase MdaB {ECO:0000250|UniProtKB:P0AEY5};
DE            EC=1.6.5.10 {ECO:0000250|UniProtKB:P0AEY5};
DE   AltName: Full=Modulator of drug activity B {ECO:0000250|UniProtKB:P0AEY5};
GN   Name=mdaB; OrderedLocusNames=c3768;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: NADPH-specific quinone reductase.
CC       {ECO:0000250|UniProtKB:P0AEY5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC         Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124;
CC         EC=1.6.5.10; Evidence={ECO:0000250|UniProtKB:P0AEY5};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P0AEY5};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AEY7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AEY5}.
CC   -!- SIMILARITY: Belongs to the oxidoreductase MdaB family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82212.1; -; Genomic_DNA.
DR   RefSeq; WP_000065430.1; NC_004431.1.
DR   AlphaFoldDB; P0AEY6; -.
DR   SMR; P0AEY6; -.
DR   STRING; 199310.c3768; -.
DR   EnsemblBacteria; AAN82212; AAN82212; c3768.
DR   GeneID; 67415030; -.
DR   KEGG; ecc:c3768; -.
DR   eggNOG; COG2249; Bacteria.
DR   HOGENOM; CLU_083846_0_0_6; -.
DR   OMA; DATIWQM; -.
DR   BioCyc; ECOL199310:C3768-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR003680; Flavodoxin_fold.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEY5"
FT   CHAIN           2..193
FT                   /note="NADPH:quinone oxidoreductase MdaB"
FT                   /id="PRO_0000096313"
FT   BINDING         16..23
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEY7"
FT   BINDING         69..72
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEY7"
FT   BINDING         108
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEY7"
FT   BINDING         124..127
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEY7"
SQ   SEQUENCE   193 AA;  21891 MW;  FEE3B4D13C2733CA CRC64;
     MSNILIINGA KKFAHSNGQL NDTLTEVADG TLRDLGHDVR IVRADSDYDV KAEVQNFLWA
     DVVIWQMPGW WMGAPWTVKK YIDDVFTEGH GTLYASDGRT RKDPSKKYGS GGLVQGKKYM
     LSLTWNAPME AFTEKDQFFH GVGVDGVYLP FHKANQFLGM EPLPTFIAND VIKMPDVPRY
     TEEYRKHLVE IFG