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P0AGE6

- CHRR_ECOLI

UniProt

P0AGE6 - CHRR_ECOLI

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Protein
Chromate reductase
Gene
chrR, yieF, b3713, JW3691
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

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.

Enzyme regulationi

Inhibited by divalent cations.

Kineticsi

Kcat is 3.7 sec(-1) for reductase activity with chromate (at pH 5 and 35 degrees Celsius. 1 Publication

). Kcat is 29 sec(-1) for reductase activity with uranate (at pH 7 and 37 degrees Celsius. 1 Publication). Kcat is 30 sec(-1) for reductase activity with chromate (at pH 7 and 37 degrees Celsius. 1 Publication).

  1. KM=108 µM for uranate (at pH 7 and 37 degrees Celsius. 1 Publication)
  2. KM=200 µM for chromate (at pH 5 and 35 degrees Celsius. 1 Publication)
  3. 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 µmol/min/mg enzyme with uranate as substrate (at pH 7 and 37 degrees Celsius. 1 Publication

)

Vmax=295 µmol/min/mg enzyme with chromate as substrate (at pH 7 and 37 degrees Celsius. 1 Publication

)

pH dependencei

Optimum pH is 5.

Temperature dependencei

Optimum temperature is 35 degrees Celsius.

Sites

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

Regions

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

GO - Molecular functioni

  1. FMN binding Source: EcoCyc
  2. oxidoreductase activity Source: EcoCyc

GO - Biological processi

  1. xenobiotic metabolic process Source: EcoCyc
Complete GO annotation...

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851Y → N: Improves chromate reductase activity compared to the wild-type enzyme.
Mutagenesisi125 – 1251R → M: Improves chromate reductase activity compared to the wild-type enzyme.
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.
Mutagenesisi146 – 1461E → T: Improves chromate reductase activity compared to the wild-type enzyme.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Chromate reductase
PRO_0000160596Add
BLAST

Proteomic databases

PaxDbiP0AGE6.
PRIDEiP0AGE6.

Expressioni

Inductioni

Induced by both chromate and the stationary phase.

Gene expression databases

GenevestigatoriP0AGE6.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Family & Domainsi

Sequence similaritiesi

Belongs to the SsuE family.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 71 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

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