UniProtKB - P0AGE6 (CHRR_ECOLI)
Protein
Quinone reductase
Gene
chrR
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the reduction of quinones (PubMed:14766567). Acts by simultaneous two-electron transfer, avoiding formation of highly reactive semiquinone intermediates and producing quinols that promote tolerance of H2O2. Quinone reduction is probably the primary biological role of ChrR (By similarity). Can also reduce toxic chromate to insoluble and less toxic Cr3+. Catalyzes the transfer of three electrons to Cr6+ producing Cr3+ and one electron to molecular oxygen without producing the toxic Cr5+ species and only producing a minimal amount of reactive oxygen species (ROS). Chromate reduction protects the cell against chromate toxicity, but is likely a secondary activity (PubMed:14766567, PubMed:17088379, PubMed:22558308). Can also reduce potassium ferricyanide, 2,6-dichloroindophenol, V5+, Mo6+, methylene blue, cytochrome c and U6+ (PubMed:14766567, PubMed:17088379). During chromate reduction, is able to use both NAD or NADP equally well (PubMed:14766567).By similarity3 Publications
Catalytic activityi
Cofactori
FMN2 PublicationsNote: Binds 1 FMN per subunit.1 Publication
Activity regulationi
May be inhibited by divalent cations.1 Publication
Kineticsi
kcat is 3.7 sec(-1) with chromate as substrate (at pH 5 and 35 degrees Celsius) (PubMed:14766567). kcat is 29 sec(-1) with uranyl as substrate (at pH 7 and 37 degrees Celsius) (PubMed:17088379). kcat is 30 sec(-1) with chromate as substrate (at pH 7 and 37 degrees Celsius) (PubMed:17088379).2 Publications
- KM=108 µM for uranyl (at pH 7 and 37 degrees Celsius)1 Publication
- KM=200 µM for chromate (at pH 5 and 35 degrees Celsius)1 Publication
- KM=376 µM for chromate (at pH 7 and 37 degrees Celsius)1 Publication
- Vmax=5 µmol/min/mg enzyme with chromate as substrate (at pH 5 and 35 degrees Celsius)1 Publication
- Vmax=213 nmol/min/mg enzyme with uranyl as substrate (at pH 7 and 37 degrees Celsius)1 Publication
- Vmax=295 nmol/min/mg enzyme with chromate as substrate (at pH 7 and 37 degrees Celsius)1 Publication
pH dependencei
Optimum pH is 5.1 Publication
Temperature dependencei
Optimum temperature is 35 degrees Celsius.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 117 | FMN1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 13 – 20 | FMN1 Publication | 8 | |
Nucleotide bindingi | 82 – 85 | FMN1 Publication | 4 |
GO - Molecular functioni
- FMN binding Source: EcoCyc
- NADH dehydrogenase (quinone) activity Source: RHEA
- NADPH dehydrogenase (quinone) activity Source: RHEA
- oxidoreductase activity Source: EcoCyc
GO - Biological processi
- xenobiotic metabolic process Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Ligand | Flavoprotein, FMN, NAD, NADP |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11723-MONOMER MetaCyc:EG11723-MONOMER |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:chrR Synonyms:yieF Ordered Locus Names:b3713, JW3691 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Disruption phenotypei
Cells lacking this gene show an increased sensitivity to chromate.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 85 | Y → N: Improves chromate reductase activity compared to the wild-type enzyme. 1 Publication | 1 | |
Mutagenesisi | 125 | R → M: Improves chromate reductase activity compared to the wild-type enzyme. 1 Publication | 1 | |
Mutagenesisi | 128 | Y → N: Improves chromate reductase activity compared to the wild-type enzyme. Increase of the affinity binding and catalytic efficiency for both chromate and uranyl. 2 Publications | 1 | |
Mutagenesisi | 146 | E → T: Improves chromate reductase activity compared to the wild-type enzyme. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000160596 | 1 – 188 | Quinone reductaseAdd BLAST | 188 |
Proteomic databases
jPOSTi | P0AGE6 |
PaxDbi | P0AGE6 |
PRIDEi | P0AGE6 |
Expressioni
Inductioni
Induced by both chromate and the stationary phase.1 Publication
Interactioni
Subunit structurei
Homotetramer. Dimer of dimers. The tetrameric configuration has a central role in chromate reductase activity.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4262171, 17 interactors |
DIPi | DIP-36041N |
IntActi | P0AGE6, 2 interactors |
STRINGi | 511145.b3713 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0AGE6 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the SsuE family.Curated
Phylogenomic databases
eggNOGi | COG0431, Bacteria |
HOGENOMi | CLU_055322_4_2_6 |
InParanoidi | P0AGE6 |
PhylomeDBi | P0AGE6 |
Family and domain databases
Gene3Di | 3.40.50.360, 1 hit |
InterProi | View protein in InterPro IPR029039, Flavoprotein-like_sf IPR005025, FMN_Rdtase-like |
Pfami | View protein in Pfam PF03358, FMN_red, 1 hit |
SUPFAMi | SSF52218, SSF52218, 1 hit |
i Sequence
Sequence statusi: Complete.
P0AGE6-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSEKLQVVTL LGSLRKGSFN GMVARTLPKI APASMEVNAL PSIADIPLYD
60 70 80 90 100
ADVQQEEGFP ATVEALAEQI RQADGVVIVT PEYNYSVPGG LKNAIDWLSR
110 120 130 140 150
LPDQPLAGKP VLIQTSSMGV IGGARCQYHL RQILVFLDAM VMNKPEFMGG
160 170 180
VIQNKVDPQT GEVIDQGTLD HLTGQLTAFG EFIQRVKI
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L10328 Genomic DNA Translation: AAA62064.1 U00096 Genomic DNA Translation: AAC76736.1 AP009048 Genomic DNA Translation: BAE77575.1 |
PIRi | B65174 |
RefSeqi | NP_418169.1, NC_000913.3 WP_001291268.1, NZ_SSZK01000035.1 |
Genome annotation databases
EnsemblBacteriai | AAC76736; AAC76736; b3713 BAE77575; BAE77575; BAE77575 |
GeneIDi | 58391852 948225 |
KEGGi | ecj:JW3691 eco:b3713 |
PATRICi | fig|1411691.4.peg.2988 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L10328 Genomic DNA Translation: AAA62064.1 U00096 Genomic DNA Translation: AAC76736.1 AP009048 Genomic DNA Translation: BAE77575.1 |
PIRi | B65174 |
RefSeqi | NP_418169.1, NC_000913.3 WP_001291268.1, NZ_SSZK01000035.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3SVL | X-ray | 2.20 | A/B | 3-188 | [»] | |
SMRi | P0AGE6 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262171, 17 interactors |
DIPi | DIP-36041N |
IntActi | P0AGE6, 2 interactors |
STRINGi | 511145.b3713 |
Proteomic databases
jPOSTi | P0AGE6 |
PaxDbi | P0AGE6 |
PRIDEi | P0AGE6 |
Genome annotation databases
EnsemblBacteriai | AAC76736; AAC76736; b3713 BAE77575; BAE77575; BAE77575 |
GeneIDi | 58391852 948225 |
KEGGi | ecj:JW3691 eco:b3713 |
PATRICi | fig|1411691.4.peg.2988 |
Organism-specific databases
EchoBASEi | EB1674 |
Phylogenomic databases
eggNOGi | COG0431, Bacteria |
HOGENOMi | CLU_055322_4_2_6 |
InParanoidi | P0AGE6 |
PhylomeDBi | P0AGE6 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11723-MONOMER MetaCyc:EG11723-MONOMER |
Miscellaneous databases
PROi | PR:P0AGE6 |
Family and domain databases
Gene3Di | 3.40.50.360, 1 hit |
InterProi | View protein in InterPro IPR029039, Flavoprotein-like_sf IPR005025, FMN_Rdtase-like |
Pfami | View protein in Pfam PF03358, FMN_red, 1 hit |
SUPFAMi | SSF52218, SSF52218, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CHRR_ECOLI | |
Accessioni | P0AGE6Primary (citable) accession number: P0AGE6 Secondary accession number(s): P31465, Q2M831 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 20, 2005 |
Last sequence update: | December 20, 2005 | |
Last modified: | April 7, 2021 | |
This is version 116 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families