CHRR_PSEPU
ID CHRR_PSEPU Reviewed; 186 AA.
AC Q93T20;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Quinone reductase {ECO:0000250|UniProtKB:Q88FF8};
DE EC=1.6.5.2 {ECO:0000250|UniProtKB:Q88FF8};
DE AltName: Full=Chromate reductase {ECO:0000305};
DE Short=CHRR;
DE EC=1.6.-.- {ECO:0000269|PubMed:10788340};
DE AltName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000250|UniProtKB:Q88FF8};
GN Name=chrR;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MK1;
RA Park C.-H., Gonzalez C., Keyhan M., Matin A.;
RT "Cloning and characterization of bacterial soluble chromate reductase genes
RT and proteins.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND ACTIVITY REGULATION.
RC STRAIN=MK1;
RX PubMed=10788340; DOI=10.1128/aem.66.5.1788-1795.2000;
RA Park C.H., Keyhan M., Wielinga B., Fendorf S., Matin A.;
RT "Purification to homogeneity and characterization of a novel Pseudomonas
RT putida chromate reductase.";
RL Appl. Environ. Microbiol. 66:1788-1795(2000).
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 (By similarity). 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 (By similarity) (PubMed:10788340). {ECO:0000250|UniProtKB:Q88FF8,
CC ECO:0000269|PubMed:10788340}.
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:0000250|UniProtKB:Q88FF8};
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:0000250|UniProtKB:Q88FF8};
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:10788340};
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:10788340};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q88FF8};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:Q88FF8};
CC -!- ACTIVITY REGULATION: Non-competitively inhibited by sulfate.
CC {ECO:0000269|PubMed:10788340}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=374 uM for chromate (at pH 5 and 50 degrees Celsius)
CC {ECO:0000269|PubMed:10788340};
CC Vmax=1.72 umol/min/mg enzyme (at pH 5 and 50 degrees Celsius)
CC {ECO:0000269|PubMed:10788340};
CC pH dependence:
CC Optimum pH is 5 for chromate reductase activity.
CC {ECO:0000269|PubMed:10788340};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius for chromate reductase
CC activity. {ECO:0000269|PubMed:10788340};
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. The tetrameric configuration
CC has a central role in chromate reductase activity.
CC {ECO:0000250|UniProtKB:Q88FF8}.
CC -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
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DR EMBL; AF375641; AAK56852.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93T20; -.
DR SMR; Q93T20; -.
DR STRING; 1240350.AMZE01000065_gene3244; -.
DR eggNOG; COG0431; Bacteria.
DR SABIO-RK; Q93T20; -.
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.
FT CHAIN 1..186
FT /note="Quinone reductase"
FT /id="PRO_0000430016"
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; 20256 MW; A8F751786868086F CRC64;
MSQVYSVAVV VGSLRKESYN RKVARALSEL APSSLALKIV EIGDLPLYNE DVEAEAPPEA
WKRFREEIRR SDAVLFVTPE HNRSVPGCLK NAIDVGSRPY GQSAWSGKPT AVVSVSPGAI
GGFGANHAVR QSLVFLDMPC MQMPEAYIGG AASLFDDSGK LNDKTRPFLQ AFVDKFASWV
KLNRAV
