ID   MDAB_HAEIN              Reviewed;         192 AA.
AC   P44803;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 93.
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; Synonyms=mda66; OrderedLocusNames=HI_0648;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC22308.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L42023; AAC22308.1; ALT_INIT; Genomic_DNA.
DR   PIR; C64084; C64084.
DR   RefSeq; NP_438808.2; NC_000907.1.
DR   RefSeq; WP_005694496.1; NC_000907.1.
DR   AlphaFoldDB; P44803; -.
DR   SMR; P44803; -.
DR   STRING; 71421.HI_0648; -.
DR   EnsemblBacteria; AAC22308; AAC22308; HI_0648.
DR   KEGG; hin:HI_0648; -.
DR   PATRIC; fig|71421.8.peg.677; -.
DR   eggNOG; COG2249; Bacteria.
DR   HOGENOM; CLU_083846_0_0_6; -.
DR   PhylomeDB; P44803; -.
DR   BioCyc; HINF71421:G1GJ1-683-MON; -.
DR   Proteomes; UP000000579; 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; Reference proteome.
FT   CHAIN           1..192
FT                   /note="NADPH:quinone oxidoreductase MdaB"
FT                   /id="PRO_0000096315"
FT   BINDING         15..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEY7"
FT   BINDING         68..71
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEY7"
FT   BINDING         107
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEY7"
FT   BINDING         123..126
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0AEY7"
SQ   SEQUENCE   192 AA;  21876 MW;  3ACF977F06A4BF0F CRC64;
     MNILLLDGGK AFGHSHGELN HTLHKKAKEV LTALGHNVKE TVIDAGYDVE AEIEKFLWMD
     AVIWQMPSWW MHEPWTVKKY IDEVLTNGHG KLYHSDGRHS VNPTEGYGTG GLLQGKKHML
     SLTWNAPIEA FTREGDFFEG KGVDVLYMHF HKLNEFLGLT RLPTFLCNDV VKSPQVEQYL
     ADYQAHLEKV FG