Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0AGE6

- CHRR_ECOLI

UniProt

P0AGE6 - CHRR_ECOLI

Protein

Chromate reductase

Gene

chrR

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the protection against chromate toxicity. 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). It can also reduce quinones, potassium ferricyanide, 2,6-dichloroindophenol, V5+, Mo6+, methylene blue and cytochrome c. The quinone reductase activity may protect against oxidative stress by preventing redox cycling of quinones which would otherwise generate ROS and by maintaining a pool of reduced quinone in the cell that is able to quench ROS directly. It is able to use both NAD or NADP equally well.4 Publications

    Catalytic activityi

    NAD(P)H + a quinone = NAD(P)+ + a hydroquinone.
    2 NAD(P)H + Cr6+ + O2 = 2 NAD(P)+ + Cr3+ + H2O2.

    Cofactori

    Binds 1 FMN per subunit.1 Publication

    Enzyme regulationi

    Inhibited by divalent cations.1 Publication

    Kineticsi

    Kcat is 3.7 sec(-1) for reductase activity with chromate (at pH 5 and 35 degrees Celsius. PubMed:14766567). Kcat is 29 sec(-1) for reductase activity with uranate (at pH 7 and 37 degrees Celsius. PubMed:17088379). Kcat is 30 sec(-1) for reductase activity with chromate (at pH 7 and 37 degrees Celsius. PubMed:17088379).

    1. KM=108 µM for uranate (at pH 7 and 37 degrees Celsius. PubMed:17088379)2 Publications
    2. KM=200 µM for chromate (at pH 5 and 35 degrees Celsius. PubMed:14766567)2 Publications
    3. KM=376 µM for chromate (at pH 7 and 37 degrees Celsius. PubMed:17088379)2 Publications

    Vmax=5 µmol/min/mg enzyme with chromate as substrate (at pH 5 and 35 degrees Celsius. PubMed:14766567)2 Publications

    Vmax=213 µmol/min/mg enzyme with uranate as substrate (at pH 7 and 37 degrees Celsius. PubMed:17088379)2 Publications

    Vmax=295 µmol/min/mg enzyme with chromate as substrate (at pH 7 and 37 degrees Celsius. PubMed:17088379)2 Publications

    pH dependencei

    Optimum pH is 5.2 Publications

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei117 – 1171FMN1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 208FMN1 Publication
    Nucleotide bindingi82 – 854FMN1 Publication

    GO - Molecular functioni

    1. FMN binding Source: EcoCyc
    2. NAD(P)H dehydrogenase (quinone) activity Source: UniProtKB-EC
    3. oxidoreductase activity Source: EcoCyc

    GO - Biological processi

    1. xenobiotic metabolic process Source: EcoCyc

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN, NAD, NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11723-MONOMER.
    ECOL316407:JW3691-MONOMER.
    MetaCyc:EG11723-MONOMER.
    RETL1328306-WGS:GSTH-4936-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromate reductase (EC:1.6.5.2)
    Short name:
    CHRR
    Alternative name(s):
    NAD(P)H dehydrogenase (quinone)
    Gene namesi
    Name:chrR
    Synonyms:yieF
    Ordered Locus Names:b3713, JW3691
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11723. chrR.

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show an increased sensitivity to chromate.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851Y → N: Improves chromate reductase activity compared to the wild-type enzyme. 1 Publication
    Mutagenesisi125 – 1251R → M: Improves chromate reductase activity compared to the wild-type enzyme. 1 Publication
    Mutagenesisi128 – 1281Y → N: Improves chromate reductase activity compared to the wild-type enzyme. Increase of the affinity binding and catalytic efficiency for both chromate and uranate. 1 Publication
    Mutagenesisi146 – 1461E → T: Improves chromate reductase activity compared to the wild-type enzyme. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 188188Chromate reductasePRO_0000160596Add
    BLAST

    Proteomic databases

    PaxDbiP0AGE6.
    PRIDEiP0AGE6.

    Expressioni

    Inductioni

    Induced by both chromate and the stationary phase.1 Publication

    Gene expression databases

    GenevestigatoriP0AGE6.

    Interactioni

    Subunit structurei

    Homotetramer. Dimer of dimers. The tetrameric configuration has a central role in chromate reductase activity.1 Publication

    Protein-protein interaction databases

    DIPiDIP-36041N.
    IntActiP0AGE6. 2 interactions.
    STRINGi511145.b3713.

    Structurei

    Secondary structure

    1
    188
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Helixi19 – 268
    Helixi27 – 293
    Beta strandi35 – 395
    Helixi51 – 566
    Helixi61 – 7212
    Beta strandi73 – 808
    Helixi89 – 9911
    Turni105 – 1084
    Beta strandi110 – 1167
    Turni120 – 1234
    Helixi124 – 13613
    Beta strandi147 – 1493
    Helixi152 – 1554
    Turni158 – 1614
    Helixi166 – 18217

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3SVLX-ray2.20A/B3-188[»]
    ProteinModelPortaliP0AGE6.
    SMRiP0AGE6. Positions 4-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SsuE family.Curated

    Phylogenomic databases

    eggNOGiCOG0431.
    HOGENOMiHOG000263119.
    OMAiIQNKVDT.
    OrthoDBiEOG6XHC2W.
    PhylomeDBiP0AGE6.

    Family and domain databases

    Gene3Di3.40.50.360. 1 hit.
    InterProiIPR029039. Flavoprotein-like.
    IPR005025. FMN_Rdtase-like.
    [Graphical view]
    PfamiPF03358. FMN_red. 1 hit.
    [Graphical view]
    SUPFAMiSSF52218. SSF52218. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AGE6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEKLQVVTL LGSLRKGSFN GMVARTLPKI APASMEVNAL PSIADIPLYD    50
    ADVQQEEGFP ATVEALAEQI RQADGVVIVT PEYNYSVPGG LKNAIDWLSR 100
    LPDQPLAGKP VLIQTSSMGV IGGARCQYHL RQILVFLDAM VMNKPEFMGG 150
    VIQNKVDPQT GEVIDQGTLD HLTGQLTAFG EFIQRVKI 188
    Length:188
    Mass (Da):20,376
    Last modified:December 20, 2005 - v1
    Checksum:i78E163CC4826905D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10328 Genomic DNA. Translation: AAA62064.1.
    U00096 Genomic DNA. Translation: AAC76736.1.
    AP009048 Genomic DNA. Translation: BAE77575.1.
    PIRiB65174.
    RefSeqiNP_418169.1. NC_000913.3.
    YP_491716.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76736; AAC76736; b3713.
    BAE77575; BAE77575; BAE77575.
    GeneIDi12933177.
    948225.
    KEGGiecj:Y75_p3455.
    eco:b3713.
    PATRICi32122921. VBIEscCol129921_3836.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491716.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3SVL X-ray 2.20 A/B 3-188 [» ]
    ProteinModelPortali P0AGE6.
    SMRi P0AGE6. Positions 4-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36041N.
    IntActi P0AGE6. 2 interactions.
    STRINGi 511145.b3713.

    Proteomic databases

    PaxDbi P0AGE6.
    PRIDEi P0AGE6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76736 ; AAC76736 ; b3713 .
    BAE77575 ; BAE77575 ; BAE77575 .
    GeneIDi 12933177.
    948225.
    KEGGi ecj:Y75_p3455.
    eco:b3713.
    PATRICi 32122921. VBIEscCol129921_3836.

    Organism-specific databases

    EchoBASEi EB1674.
    EcoGenei EG11723. chrR.

    Phylogenomic databases

    eggNOGi COG0431.
    HOGENOMi HOG000263119.
    OMAi IQNKVDT.
    OrthoDBi EOG6XHC2W.
    PhylomeDBi P0AGE6.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11723-MONOMER.
    ECOL316407:JW3691-MONOMER.
    MetaCyc:EG11723-MONOMER.
    RETL1328306-WGS:GSTH-4936-MONOMER.

    Miscellaneous databases

    PROi P0AGE6.

    Gene expression databases

    Genevestigatori P0AGE6.

    Family and domain databases

    Gene3Di 3.40.50.360. 1 hit.
    InterProi IPR029039. Flavoprotein-like.
    IPR005025. FMN_Rdtase-like.
    [Graphical view ]
    Pfami PF03358. FMN_red. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52218. SSF52218. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
      Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
      Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Chromate-reducing properties of soluble flavoproteins from Pseudomonas putida and Escherichia coli."
      Ackerley D.F., Gonzalez C.F., Park C.H., Blake R. II, Keyhan M., Matin A.
      Appl. Environ. Microbiol. 70:873-882(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION, INDUCTION, COFACTOR.
    5. "Analysis of novel soluble chromate and uranyl reductases and generation of an improved enzyme by directed evolution."
      Barak Y., Ackerley D.F., Dodge C.J., Banwari L., Alex C., Francis A.J., Matin A.
      Appl. Environ. Microbiol. 72:7074-7082(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-128.
    6. "Effect of chromate stress on Escherichia coli K-12."
      Ackerley D.F., Barak Y., Lynch S.V., Curtin J., Matin A.
      J. Bacteriol. 188:3371-3381(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "Crystal structure of ChrR--a quinone reductase with the capacity to reduce chromate."
      Eswaramoorthy S., Poulain S., Hienerwadel R., Bremond N., Sylvester M.D., Zhang Y.B., Berthomieu C., Van Der Lelie D., Matin A.
      PLoS ONE 7:E36017-E36017(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 3-188 IN COMPLEX WITH FMN, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-85; ARG-125 AND GLU-146, SUBUNIT.
      Strain: K12.

    Entry informationi

    Entry nameiCHRR_ECOLI
    AccessioniPrimary (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: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3