QOR2_ECOLI
ID QOR2_ECOLI Reviewed; 286 AA.
AC P39315; Q2M694;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Quinone oxidoreductase 2;
DE EC=1.6.5.2;
GN Name=qorB; Synonyms=qor2, ytfG; OrderedLocusNames=b4211, JW4169;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(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 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC
RP ACTIVITY, SUBUNIT, MUTAGENESIS OF TRP-139; TYR-140 AND ASN-143,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=18455185; DOI=10.1016/j.jmb.2008.04.003;
RA Kim I.K., Yim H.S., Kim M.K., Kim D.W., Kim Y.M., Cha S.S., Kang S.O.;
RT "Crystal structure of a new type of NADPH-dependent quinone oxidoreductase
RT (QOR2) from Escherichia coli.";
RL J. Mol. Biol. 379:372-384(2008).
CC -!- FUNCTION: Quinone oxidoreductase that may play some additional role
CC beyond quinone reduction. Potential redox sensor protein.
CC Overexpression induces retardation of growth.
CC {ECO:0000269|PubMed:18455185}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000269|PubMed:18455185};
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; EC=1.6.5.2;
CC Evidence={ECO:0000269|PubMed:18455185};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=65.6 uM for methyl-1,4-benzoquinone (MBQ)
CC {ECO:0000269|PubMed:18455185};
CC KM=18 uM for NADPH {ECO:0000269|PubMed:18455185};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18455185}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; U14003; AAA97107.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77168.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78212.1; -; Genomic_DNA.
DR PIR; S56436; S56436.
DR RefSeq; NP_418632.1; NC_000913.3.
DR RefSeq; WP_000560561.1; NZ_LN832404.1.
DR PDB; 2ZCU; X-ray; 1.80 A; A=1-286.
DR PDB; 2ZCV; X-ray; 2.30 A; A=1-286.
DR PDBsum; 2ZCU; -.
DR PDBsum; 2ZCV; -.
DR AlphaFoldDB; P39315; -.
DR SMR; P39315; -.
DR BioGRID; 4263443; 14.
DR DIP; DIP-12935N; -.
DR IntAct; P39315; 4.
DR STRING; 511145.b4211; -.
DR jPOST; P39315; -.
DR PaxDb; P39315; -.
DR PRIDE; P39315; -.
DR DNASU; 948731; -.
DR EnsemblBacteria; AAC77168; AAC77168; b4211.
DR EnsemblBacteria; BAE78212; BAE78212; BAE78212.
DR GeneID; 948731; -.
DR KEGG; ecj:JW4169; -.
DR KEGG; eco:b4211; -.
DR PATRIC; fig|1411691.4.peg.2490; -.
DR EchoBASE; EB2400; -.
DR eggNOG; COG0702; Bacteria.
DR HOGENOM; CLU_007383_10_4_6; -.
DR InParanoid; P39315; -.
DR OMA; NGWYHEN; -.
DR PhylomeDB; P39315; -.
DR BioCyc; EcoCyc:G7868-MON; -.
DR BioCyc; MetaCyc:G7868-MON; -.
DR BRENDA; 1.6.5.2; 2026.
DR SABIO-RK; P39315; -.
DR EvolutionaryTrace; P39315; -.
DR PRO; PR:P39315; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:EcoCyc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..286
FT /note="Quinone oxidoreductase 2"
FT /id="PRO_0000169825"
FT BINDING 6..11
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18455185"
FT BINDING 33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18455185"
FT BINDING 73..75
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18455185"
FT BINDING 138..143
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18455185"
FT BINDING 171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18455185"
FT MUTAGEN 139
FT /note="W->A,I: 3-fold increase in the Km for methyl-1,4-
FT benzoquinone."
FT /evidence="ECO:0000269|PubMed:18455185"
FT MUTAGEN 139
FT /note="W->F: Almost no change in the Km for methyl-1,4-
FT benzoquinone."
FT /evidence="ECO:0000269|PubMed:18455185"
FT MUTAGEN 140
FT /note="Y->A,I: Almost complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:18455185"
FT MUTAGEN 140
FT /note="Y->F: No change."
FT /evidence="ECO:0000269|PubMed:18455185"
FT MUTAGEN 143
FT /note="N->A,L: 6-fold increase in the Km for methyl-1,4-
FT benzoquinone. No change in affinity for NADPH."
FT /evidence="ECO:0000269|PubMed:18455185"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:2ZCU"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2ZCU"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2ZCU"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:2ZCU"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:2ZCU"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2ZCU"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:2ZCU"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:2ZCU"
FT TURN 105..109
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:2ZCU"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:2ZCU"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:2ZCU"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2ZCU"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:2ZCU"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 238..252
FT /evidence="ECO:0007829|PDB:2ZCU"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:2ZCU"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2ZCU"
SQ SEQUENCE 286 AA; 29734 MW; 643C7A74CEE13CEA CRC64;
MIAITGATGQ LGHYVIESLM KTVPASQIVA IVRNPAKAQA LAAQGITVRQ ADYGDEAALT
SALQGVEKLL LISSSEVGQR APQHRNVINA AKAAGVKFIA YTSLLHADTS PLGLADEHIE
TEKMLADSGI VYTLLRNGWY SENYLASAPA ALEHGVFIGA AGDGKIASAT RADYAAAAAR
VISEAGHEGK VYELAGDSAW TLTQLAAELT KQSGKQVTYQ NLSEADFAAA LKSVGLPDGL
ADMLADSDVG ASKGGLFDDS KTLSKLIGHP TTTLAESVSH LFNVNN
