MDAB_ECO57
ID MDAB_ECO57 Reviewed; 193 AA.
AC P0AEY7; P40717;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=NADPH:quinone oxidoreductase MdaB {ECO:0000305};
DE EC=1.6.5.10 {ECO:0000250|UniProtKB:P0AEY5};
DE AltName: Full=Modulator of drug activity B {ECO:0000303|PubMed:16511004};
GN Name=mdaB {ECO:0000303|PubMed:16511004}; OrderedLocusNames=Z4379, ECs3910;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP SUBUNIT, AND CRYSTALLIZATION.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=16511004; DOI=10.1107/s1744309105001545;
RA Adams M.A., Iannuzzi P., Jia Z.;
RT "MdaB from Escherichia coli: cloning, purification, crystallization and
RT preliminary X-ray analysis.";
RL Acta Crystallogr. F 61:235-238(2005).
RN [4] {ECO:0007744|PDB:2B3D}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-193 OF APOENZYME AND IN COMPLEX
RP WITH FAD, COFACTOR, AND SUBUNIT.
RX PubMed=16630630; DOI=10.1016/j.jmb.2006.03.053;
RA Adams M.A., Jia Z.;
RT "Modulator of drug activity B from Escherichia coli: crystal structure of a
RT prokaryotic homologue of DT-diaphorase.";
RL J. Mol. Biol. 359:455-465(2006).
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:0000269|PubMed:16630630};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16511004,
CC ECO:0000269|PubMed:16630630}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AEY5}.
CC -!- SIMILARITY: Belongs to the oxidoreductase MdaB family. {ECO:0000305}.
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DR EMBL; AE005174; AAG58161.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37333.1; -; Genomic_DNA.
DR PIR; E85962; E85962.
DR PIR; F91117; F91117.
DR RefSeq; NP_311937.1; NC_002695.1.
DR RefSeq; WP_000065430.1; NZ_SWKA01000005.1.
DR PDB; 2AMJ; X-ray; 1.80 A; A/B/C/D=2-193.
DR PDB; 2B3D; X-ray; 2.10 A; A/B=2-193.
DR PDBsum; 2AMJ; -.
DR PDBsum; 2B3D; -.
DR AlphaFoldDB; P0AEY7; -.
DR SMR; P0AEY7; -.
DR STRING; 155864.EDL933_4248; -.
DR EnsemblBacteria; AAG58161; AAG58161; Z4379.
DR EnsemblBacteria; BAB37333; BAB37333; ECs_3910.
DR GeneID; 67415030; -.
DR GeneID; 916264; -.
DR KEGG; ece:Z4379; -.
DR KEGG; ecs:ECs_3910; -.
DR PATRIC; fig|386585.9.peg.4078; -.
DR eggNOG; COG2249; Bacteria.
DR HOGENOM; CLU_083846_0_0_6; -.
DR OMA; DATIWQM; -.
DR EvolutionaryTrace; P0AEY7; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; Oxidoreductase;
KW Reference proteome.
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_0000096314"
FT BINDING 16..23
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16630630,
FT ECO:0007744|PDB:2B3D"
FT BINDING 69..72
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16630630,
FT ECO:0007744|PDB:2B3D"
FT BINDING 108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16630630,
FT ECO:0007744|PDB:2B3D"
FT BINDING 124..127
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16630630,
FT ECO:0007744|PDB:2B3D"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2AMJ"
FT HELIX 19..34
FT /evidence="ECO:0007829|PDB:2AMJ"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:2AMJ"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:2AMJ"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:2AMJ"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:2AMJ"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:2AMJ"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2AMJ"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:2AMJ"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2AMJ"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2AMJ"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:2AMJ"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:2AMJ"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2AMJ"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:2AMJ"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2AMJ"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:2AMJ"
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
