CHRR_PSEPK
ID CHRR_PSEPK Reviewed; 186 AA.
AC Q88FF8; Q7BD45; Q93T19;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Quinone reductase {ECO:0000305};
DE EC=1.6.5.2 {ECO:0000269|PubMed:15840577};
DE AltName: Full=Chromate reductase {ECO:0000305};
DE Short=CHRR;
DE EC=1.6.-.- {ECO:0000269|PubMed:14766567};
DE AltName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000305};
GN Name=chrR {ECO:0000303|PubMed:14766567}; OrderedLocusNames=PP_4138;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE,
RP ACTIVITY REGULATION, INDUCTION, AND COFACTOR.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=15840577; DOI=10.1074/jbc.m501654200;
RA Gonzalez C.F., Ackerley D.F., Lynch S.V., Matin A.;
RT "ChrR, a soluble quinone reductase of Pseudomonas putida that defends
RT against H2O2.";
RL J. Biol. Chem. 280:22590-22595(2005).
CC -!- FUNCTION: Catalyzes the reduction of quinones. Acts by simultaneous
CC two-electron transfer, avoiding formation of highly reactive
CC semiquinone intermediates and producing quinols that promote tolerance
CC of H(2)O(2). Quinone reduction is probably the primary biological role
CC of ChrR (PubMed:15840577). Can also reduce toxic chromate to insoluble
CC and less toxic Cr(3+). Catalyzes the transfer of three electrons to
CC Cr(6+) producing Cr(3+) and one electron to molecular oxygen. This
CC reaction produces transiently a minimal amount of the toxic Cr(5+)
CC species and reactive oxygen species (ROS). Chromate reduction protects
CC the cell against chromate toxicity, but is likely a secondary activity
CC (PubMed:14766567, PubMed:15840577). Can also reduce potassium
CC ferricyanide and 2,6-dichloroindophenol (PubMed:14766567). During
CC chromate reduction, displays an eightfold preference for NADH over
CC NADPH (PubMed:14766567). {ECO:0000269|PubMed:14766567,
CC ECO:0000269|PubMed:15840577}.
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:15840577};
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:15840577};
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};
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};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:14766567};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:P0AGE6};
CC -!- ACTIVITY REGULATION: May be inhibited by divalent cations.
CC {ECO:0000269|PubMed:14766567}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=110 uM for benzoquinone (at pH 7.5 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:15840577};
CC KM=230 uM for menaquinone (at pH 8.0 and 60 degrees Celsius)
CC {ECO:0000269|PubMed:15840577};
CC KM=210 uM for duroquinone (at pH 8.0 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:15840577};
CC KM=120 uM for coenzyme Q1 (at pH 8.5 and 60 degrees Celsius)
CC {ECO:0000269|PubMed:15840577};
CC KM=260 uM for chromate (at pH 5 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:14766567};
CC Vmax=1400 umol/min/mg enzyme with benzoquinone as substrate (at pH
CC 7.5 and 70 degrees Celsius) {ECO:0000269|PubMed:15840577};
CC Vmax=660 umol/min/mg enzyme with menaquinone as substrate (at pH 8.0
CC and 60 degrees Celsius) {ECO:0000269|PubMed:15840577};
CC Vmax=37 umol/min/mg enzyme with duroquinone as substrate (at pH 8.0
CC and 70 degrees Celsius) {ECO:0000269|PubMed:15840577};
CC Vmax=9.6 umol/min/mg enzyme with coenzyme Q1 as substrate (at pH 8.5
CC and 60 degrees Celsius) {ECO:0000269|PubMed:15840577};
CC Vmax=8.8 umol/min/mg enzyme with chromate as substrate (at pH 5 and
CC 70 degrees Celsius) {ECO:0000269|PubMed:14766567};
CC Note=kcat is 930 sec(-1) with benzoquinone as substrate (at pH 7.5
CC and 70 degrees Celsius) (PubMed:15840577). kcat is 440 sec(-1) with
CC menaquinone as substrate (at pH 8.0 and 60 degrees Celsius)
CC (PubMed:15840577). kcat is 25 sec(-1) with duroquinone as substrate
CC (at pH 8.0 and 70 degrees Celsius) (PubMed:15840577). kcat is 6.4
CC sec(-1) with coenzyme Q1 as substrate (at pH 8.5 and 60 degrees
CC Celsius) (PubMed:15840577). kcat is 5.8 sec(-1) with chromate as
CC substrate (at pH 5 and 70 degrees Celsius) (PubMed:14766567).
CC {ECO:0000269|PubMed:14766567, ECO:0000269|PubMed:15840577};
CC pH dependence:
CC Optimum pH is 5 for chromate reductase activity.
CC {ECO:0000269|PubMed:14766567};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius for chromate reductase
CC activity. {ECO:0000269|PubMed:14766567};
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. The tetrameric configuration
CC has a central role in chromate reductase activity.
CC {ECO:0000250|UniProtKB:P0AGE6}.
CC -!- INDUCTION: Induced by H(2)O(2) (PubMed:15840577). Induced by both
CC chromate and the stationary phase (PubMed:14766567).
CC {ECO:0000269|PubMed:14766567, ECO:0000269|PubMed:15840577}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are inhibited by chromate
CC to a greater extent than the wild-type. {ECO:0000269|PubMed:14766567}.
CC -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
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DR EMBL; AF375642; AAK56853.1; -; Genomic_DNA.
DR EMBL; AE015451; AAN69721.1; -; Genomic_DNA.
DR RefSeq; NP_746257.1; NC_002947.4.
DR RefSeq; WP_003251456.1; NC_002947.4.
DR AlphaFoldDB; Q88FF8; -.
DR SMR; Q88FF8; -.
DR STRING; 160488.PP_4138; -.
DR EnsemblBacteria; AAN69721; AAN69721; PP_4138.
DR KEGG; ppu:PP_4138; -.
DR PATRIC; fig|160488.4.peg.4397; -.
DR eggNOG; COG0431; Bacteria.
DR HOGENOM; CLU_055322_4_2_6; -.
DR OMA; YGGVWAQ; -.
DR PhylomeDB; Q88FF8; -.
DR BioCyc; MetaCyc:G1G01-4405-MON; -.
DR BioCyc; PPUT160488:G1G01-4405-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
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 Flavoprotein; FMN; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..186
FT /note="Quinone reductase"
FT /id="PRO_0000430015"
FT BINDING 13..20
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AGE6"
FT BINDING 80..83
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AGE6"
FT BINDING 116
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AGE6"
SQ SEQUENCE 186 AA; 20354 MW; 9C01013614AF5D6A CRC64;
MSQVYSVAVV VGSLRKESYN RKVARALSEL APSSLALKIV EIGDLPLYNE DIEAEAPPET
WKRFRDEIRR SDAVLFVTPE YNRSVPGCLK NAIDVGSRPY GQSAWSGKPT AVVSVSPGAI
GGFGANHAVR QSLVFLDMPC MQMPEAYLGG AASLFEDSGK LNDKTRPFLQ AFVDRFASWV
KLNRAV
