CHRR_ECOLI
ID CHRR_ECOLI Reviewed; 188 AA.
AC P0AGE6; P31465; Q2M831;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Quinone reductase {ECO:0000305};
DE EC=1.6.5.2 {ECO:0000269|PubMed:14766567};
DE AltName: Full=Chromate reductase {ECO:0000305};
DE Short=CHRR;
DE EC=1.6.-.- {ECO:0000269|PubMed:14766567, ECO:0000269|PubMed:17088379, ECO:0000269|PubMed:22558308};
DE AltName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000305};
GN Name=chrR; Synonyms=yieF; OrderedLocusNames=b3713, JW3691;
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=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, INDUCTION, AND COFACTOR.
RX PubMed=14766567; DOI=10.1128/aem.70.2.873-882.2004;
RA Ackerley D.F., Gonzalez C.F., Park C.H., Blake R. II, Keyhan M., Matin A.;
RT "Chromate-reducing properties of soluble flavoproteins from Pseudomonas
RT putida and Escherichia coli.";
RL Appl. Environ. Microbiol. 70:873-882(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-128.
RX PubMed=17088379; DOI=10.1128/aem.01334-06;
RA Barak Y., Ackerley D.F., Dodge C.J., Banwari L., Alex C., Francis A.J.,
RA Matin A.;
RT "Analysis of novel soluble chromate and uranyl reductases and generation of
RT an improved enzyme by directed evolution.";
RL Appl. Environ. Microbiol. 72:7074-7082(2006).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=16621832; DOI=10.1128/jb.188.9.3371-3381.2006;
RA Ackerley D.F., Barak Y., Lynch S.V., Curtin J., Matin A.;
RT "Effect of chromate stress on Escherichia coli K-12.";
RL J. Bacteriol. 188:3371-3381(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 3-188 IN COMPLEX WITH FMN,
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-85; ARG-125; TYR-128 AND
RP GLU-146, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=22558308; DOI=10.1371/journal.pone.0036017;
RA Eswaramoorthy S., Poulain S., Hienerwadel R., Bremond N., Sylvester M.D.,
RA Zhang Y.B., Berthomieu C., Van Der Lelie D., Matin A.;
RT "Crystal structure of ChrR--a quinone reductase with the capacity to reduce
RT chromate.";
RL PLoS ONE 7:E36017-E36017(2012).
CC -!- FUNCTION: Catalyzes the reduction of quinones (PubMed:14766567). Acts
CC by simultaneous two-electron transfer, avoiding formation of highly
CC reactive semiquinone intermediates and producing quinols that promote
CC tolerance of H(2)O(2). Quinone reduction is probably the primary
CC biological role of ChrR (By similarity). Can also reduce toxic chromate
CC to insoluble and less toxic Cr(3+). Catalyzes the transfer of three
CC electrons to Cr(6+) producing Cr(3+) and one electron to molecular
CC oxygen without producing the toxic Cr(5+) species and only producing a
CC minimal amount of reactive oxygen species (ROS). Chromate reduction
CC protects the cell against chromate toxicity, but is likely a secondary
CC activity (PubMed:14766567, PubMed:17088379, PubMed:22558308). Can also
CC reduce potassium ferricyanide, 2,6-dichloroindophenol, V(5+), Mo(6+),
CC methylene blue, cytochrome c and U(6+) (PubMed:14766567,
CC PubMed:17088379). During chromate reduction, is able to use both NAD or
CC NADP equally well (PubMed:14766567). {ECO:0000250|UniProtKB:Q88FF8,
CC ECO:0000269|PubMed:14766567, ECO:0000269|PubMed:17088379,
CC ECO:0000269|PubMed:22558308}.
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:14766567};
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:14766567};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cr(6+) + 2 NADH + O2 = Cr(3+) + 2 H(+) + 2 NAD(+) +
CC superoxide; Xref=Rhea:RHEA:44372, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:18421, ChEBI:CHEBI:33007,
CC ChEBI:CHEBI:49544, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:14766567, ECO:0000269|PubMed:17088379,
CC ECO:0000269|PubMed:22558308};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cr(6+) + 2 NADPH + O2 = Cr(3+) + 2 H(+) + 2 NADP(+) +
CC superoxide; Xref=Rhea:RHEA:44368, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:18421, ChEBI:CHEBI:33007,
CC ChEBI:CHEBI:49544, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:14766567, ECO:0000269|PubMed:17088379,
CC ECO:0000269|PubMed:22558308};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:14766567, ECO:0000269|PubMed:22558308};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:22558308};
CC -!- ACTIVITY REGULATION: May be inhibited by divalent cations.
CC {ECO:0000269|PubMed:14766567}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=108 uM for uranyl (at pH 7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17088379};
CC KM=200 uM for chromate (at pH 5 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:14766567};
CC KM=376 uM for chromate (at pH 7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17088379};
CC Vmax=5 umol/min/mg enzyme with chromate as substrate (at pH 5 and 35
CC degrees Celsius) {ECO:0000269|PubMed:14766567};
CC Vmax=213 nmol/min/mg enzyme with uranyl as substrate (at pH 7 and 37
CC degrees Celsius) {ECO:0000269|PubMed:17088379};
CC Vmax=295 nmol/min/mg enzyme with chromate as substrate (at pH 7 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:17088379};
CC Note=kcat is 3.7 sec(-1) with chromate as substrate (at pH 5 and 35
CC degrees Celsius) (PubMed:14766567). kcat is 29 sec(-1) with uranyl as
CC substrate (at pH 7 and 37 degrees Celsius) (PubMed:17088379). kcat is
CC 30 sec(-1) with chromate as substrate (at pH 7 and 37 degrees
CC Celsius) (PubMed:17088379). {ECO:0000269|PubMed:14766567,
CC ECO:0000269|PubMed:17088379};
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:14766567};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:14766567};
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. The tetrameric configuration
CC has a central role in chromate reductase activity.
CC {ECO:0000269|PubMed:22558308}.
CC -!- INDUCTION: Induced by both chromate and the stationary phase.
CC {ECO:0000269|PubMed:14766567}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an increased
CC sensitivity to chromate. {ECO:0000269|PubMed:16621832}.
CC -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
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DR EMBL; L10328; AAA62064.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76736.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77575.1; -; Genomic_DNA.
DR PIR; B65174; B65174.
DR RefSeq; NP_418169.1; NC_000913.3.
DR RefSeq; WP_001291268.1; NZ_SSZK01000035.1.
DR PDB; 3SVL; X-ray; 2.20 A; A/B=3-188.
DR PDBsum; 3SVL; -.
DR AlphaFoldDB; P0AGE6; -.
DR SMR; P0AGE6; -.
DR BioGRID; 4262171; 17.
DR DIP; DIP-36041N; -.
DR IntAct; P0AGE6; 2.
DR STRING; 511145.b3713; -.
DR jPOST; P0AGE6; -.
DR PaxDb; P0AGE6; -.
DR PRIDE; P0AGE6; -.
DR EnsemblBacteria; AAC76736; AAC76736; b3713.
DR EnsemblBacteria; BAE77575; BAE77575; BAE77575.
DR GeneID; 58391852; -.
DR GeneID; 948225; -.
DR KEGG; ecj:JW3691; -.
DR KEGG; eco:b3713; -.
DR PATRIC; fig|1411691.4.peg.2988; -.
DR EchoBASE; EB1674; -.
DR eggNOG; COG0431; Bacteria.
DR HOGENOM; CLU_055322_4_2_6; -.
DR InParanoid; P0AGE6; -.
DR OMA; YGGVWAQ; -.
DR PhylomeDB; P0AGE6; -.
DR BioCyc; EcoCyc:EG11723-MON; -.
DR BioCyc; MetaCyc:EG11723-MON; -.
DR PRO; PR:P0AGE6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0034567; F:chromate reductase activity; IDA:EcoCyc.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; 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:0016491; F:oxidoreductase activity; IDA:EcoCyc.
DR GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
DR GO; GO:0006805; P:xenobiotic metabolic process; IMP:EcoCyc.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..188
FT /note="Quinone reductase"
FT /id="PRO_0000160596"
FT BINDING 13..20
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:22558308"
FT BINDING 82..85
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:22558308"
FT BINDING 117
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:22558308"
FT MUTAGEN 85
FT /note="Y->N: Improves chromate reductase activity compared
FT to the wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:22558308"
FT MUTAGEN 125
FT /note="R->M: Improves chromate reductase activity compared
FT to the wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:22558308"
FT MUTAGEN 128
FT /note="Y->N: Improves chromate reductase activity compared
FT to the wild-type enzyme. Increase of the affinity binding
FT and catalytic efficiency for both chromate and uranyl."
FT /evidence="ECO:0000269|PubMed:17088379,
FT ECO:0000269|PubMed:22558308"
FT MUTAGEN 146
FT /note="E->T: Improves chromate reductase activity compared
FT to the wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:22558308"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:3SVL"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:3SVL"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3SVL"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3SVL"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:3SVL"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:3SVL"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:3SVL"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:3SVL"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:3SVL"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:3SVL"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:3SVL"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:3SVL"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3SVL"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:3SVL"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:3SVL"
FT HELIX 166..182
FT /evidence="ECO:0007829|PDB:3SVL"
SQ SEQUENCE 188 AA; 20376 MW; 78E163CC4826905D CRC64;
MSEKLQVVTL LGSLRKGSFN GMVARTLPKI APASMEVNAL PSIADIPLYD ADVQQEEGFP
ATVEALAEQI RQADGVVIVT PEYNYSVPGG LKNAIDWLSR LPDQPLAGKP VLIQTSSMGV
IGGARCQYHL RQILVFLDAM VMNKPEFMGG VIQNKVDPQT GEVIDQGTLD HLTGQLTAFG
EFIQRVKI
