(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 141.
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}.
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   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; ENOG4105ECR; Bacteria.
DR   eggNOG; COG0702; LUCA.
DR   HOGENOM; HOG000035268; -.
DR   InParanoid; P39315; -.
DR   KO; K19267; -.
DR   PhylomeDB; P39315; -.
DR   BioCyc; EcoCyc:G7868-MONOMER; -.
DR   BioCyc; ECOL316407:JW4169-MONOMER; -.
DR   BioCyc; MetaCyc:G7868-MONOMER; -.
DR   BRENDA; 1.6.5.2; 2026.
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:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
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;
DR   PRODOM; P39315.
DR   SWISS-2DPAGE; P39315.
KW   3D-structure; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..286
FT                   /note="Quinone oxidoreductase 2"
FT                   /id="PRO_0000169825"
FT   NP_BIND         6..11
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:18455185"
FT   NP_BIND         73..75
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:18455185"
FT   NP_BIND         138..143
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:18455185"
FT   BINDING         33
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:18455185"
FT   BINDING         171
FT                   /note="NADP"
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:0000244|PDB:2ZCU"
FT   HELIX           10..19
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   TURN            20..22
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           25..27
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   STRAND          28..33
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   TURN            35..37
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           39..43
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   STRAND          47..50
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           56..62
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   TURN            63..65
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   STRAND          67..71
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           83..94
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   STRAND          98..104
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   TURN            105..109
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           115..128
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   STRAND          130..137
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           141..145
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           148..154
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   STRAND          156..160
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           171..183
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   STRAND          184..186
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   STRAND          191..194
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           202..213
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   STRAND          218..221
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           224..231
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           238..252
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   TURN            253..256
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           262..267
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           274..279
FT                   /evidence="ECO:0000244|PDB:2ZCU"
FT   HELIX           280..282
FT                   /evidence="ECO:0000244|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
//

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