MDAB_ECOLI
ID MDAB_ECOLI Reviewed; 193 AA.
AC P0AEY5; P40717; Q2M9H2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=NADPH:quinone oxidoreductase MdaB {ECO:0000305};
DE EC=1.6.5.10 {ECO:0000269|PubMed:8611590};
DE AltName: Full=Modulator of drug activity B {ECO:0000303|PubMed:7568050};
GN Name=mdaB {ECO:0000303|PubMed:7568050};
GN Synonyms=mda66 {ECO:0000303|PubMed:8611590};
GN OrderedLocusNames=b3028, JW2996;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OVEREXPRESSION.
RX PubMed=7568050; DOI=10.1073/pnas.92.19.8950;
RA Chatterjee P.K., Sternberg N.L.;
RT "A general genetic approach in Escherichia coli for determining the
RT mechanism(s) of action of tumoricidal agents: application to DMP 840, a
RT tumoricidal agent.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8950-8954(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=8611590; DOI=10.1016/0005-2728(95)00138-7;
RA Hayashi M., Ohzeki H., Shimada H., Unemoto T.;
RT "NADPH-specific quinone reductase is induced by 2-methylene-4-butyrolactone
RT in Escherichia coli.";
RL Biochim. Biophys. Acta 1273:165-170(1996).
CC -!- FUNCTION: NADPH-specific quinone reductase. Is most active with quinone
CC derivatives and ferricyanide as electron acceptors. Can use menadione,
CC 1,4-naphthoquinone and 1,4-benzoquinone. {ECO:0000269|PubMed:8611590}.
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:0000269|PubMed:8611590};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:8611590};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.5 uM for NADPH {ECO:0000269|PubMed:8611590};
CC KM=6 uM for menadione {ECO:0000269|PubMed:8611590};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:8611590};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AEY7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8611590}.
CC -!- INDUCTION: Induced by 2-methylene-4-butyrolactone (MBL).
CC {ECO:0000269|PubMed:8611590}.
CC -!- MISCELLANEOUS: Overexpression leads to increased resistance to the
CC tumoricidal agent DMP 840. {ECO:0000269|PubMed:7568050}.
CC -!- SIMILARITY: Belongs to the oxidoreductase MdaB family. {ECO:0000305}.
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DR EMBL; U18656; AAC43451.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69196.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76064.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77084.1; -; Genomic_DNA.
DR PIR; I80319; I80319.
DR RefSeq; NP_417500.1; NC_000913.3.
DR RefSeq; WP_000065430.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P0AEY5; -.
DR SMR; P0AEY5; -.
DR BioGRID; 4263034; 19.
DR IntAct; P0AEY5; 3.
DR STRING; 511145.b3028; -.
DR jPOST; P0AEY5; -.
DR PaxDb; P0AEY5; -.
DR PRIDE; P0AEY5; -.
DR EnsemblBacteria; AAC76064; AAC76064; b3028.
DR EnsemblBacteria; BAE77084; BAE77084; BAE77084.
DR GeneID; 67415030; -.
DR GeneID; 947512; -.
DR KEGG; ecj:JW2996; -.
DR KEGG; eco:b3028; -.
DR PATRIC; fig|1411691.4.peg.3703; -.
DR EchoBASE; EB2524; -.
DR eggNOG; COG2249; Bacteria.
DR HOGENOM; CLU_083846_0_0_6; -.
DR InParanoid; P0AEY5; -.
DR OMA; DATIWQM; -.
DR PhylomeDB; P0AEY5; -.
DR BioCyc; EcoCyc:EG12656-MON; -.
DR BioCyc; MetaCyc:EG12656-MON; -.
DR EvolutionaryTrace; P0AEY5; -.
DR PRO; PR:P0AEY5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8611590"
FT CHAIN 2..193
FT /note="NADPH:quinone oxidoreductase MdaB"
FT /id="PRO_0000096312"
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
