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P77526 (YFCG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disulfide-bond oxidoreductase YfcG

EC=1.8.4.-
Alternative name(s):
GSH-dependent disulfide-bond oxidoreductase YfcG
GST N1-1
GST-like protein YfcG
Organic hydroperoxidase
EC=1.11.1.-
Gene names
Name:yfcG
Ordered Locus Names:b2302, JW2299
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exhibits a very robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H2O2, tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the nucleophilic substrate. Is involved in defense against oxidative stress, probably via its peroxidase activity. Ref.4 Ref.6

Subunit structure

Homodimer Probable. Ref.6

Disruption phenotype

Deletion of yfcG decreases the resistance of the bacteria to hydrogen peroxide. Ref.4

Miscellaneous

The reductase activity of YfcG is unique in that no sulfhydryl groups in the protein appear to be covalently involved in the redox chemistry (Ref.6).

Glutathionylspermidine (GspSH) binds YfcG about 10 times more tightly than GSH. Moreover, GSSG binds 100 times more tightly than GSH and 10 times more tightly than the GSH analog, GSO3- (Ref.6).

Sequence similarities

Belongs to the GST superfamily. Nu-class GSH transferase family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

kcat is 180 sec(-1) for the disulfide-bond reductase reaction toward 2-hydroxyethyl disulfide. kcat is 0.27 sec(-1) for the hydroperoxidase reaction with cumene hydroperoxide. kcat is 0.1 sec(-1) for the GSH transferase reaction with chloro-2,4-dinitrobenzene (CDNB) as substrate.

KM=1.6 mM for glutathione (when assaying the disulfide-bond reductase activity with 2-hydroxyethyl disulfide) Ref.6

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Disulfide-bond oxidoreductase YfcG
PRO_0000186016

Regions

Domain1 – 8787GST N-terminal
Domain90 – 215126GST C-terminal
Region71 – 722Glutathione 1 binding

Sites

Binding site111Glutathione 1
Binding site381Glutathione 1
Binding site521Glutathione 1; via amide nitrogen and carbonyl oxygen
Binding site1321Glutathione 2

Experimental info

Mutagenesis91T → A: No effect on GSH transferase activity. Ref.4
Mutagenesis111N → A: Loss of GSH transferase activity. Ref.4
Mutagenesis141K → A: 10-fold reduction in GSH transferase activity. Ref.4
Mutagenesis1661C → A: No effect on disulfide-bond reductase activity. Ref.6

Secondary structure

.................................. 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P77526 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 058CEBAC879A3050

FASTA21524,516
        10         20         30         40         50         60 
MIDLYFAPTP NGHKITLFLE EAELDYRLIK VDLGKGGQFR PEFLRISPNN KIPAIVDHSP 

        70         80         90        100        110        120 
ADGGEPLSLF ESGAILLYLA EKTGLFLSHE TRERAATLQW LFWQVGGLGP MLGQNHHFNH 

       130        140        150        160        170        180 
AAPQTIPYAI ERYQVETQRL YHVLNKRLEN SPWLGGENYS IADIACWPWV NAWTRQRIDL 

       190        200        210 
AMYPAVKNWH ERIRSRPATG QALLKAQLGD ERSDS 

« Hide

References

« Hide 'large scale' references
[1]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress."
Kanai T., Takahashi K., Inoue H.
J. Biochem. 140:703-711(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEFENSE AGAINST OXIDATIVE STRESS, GSH TRANSFERASE ACTIVITY, PEROXIDASE ACTIVITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF THR-9; ASN-11 AND LYS-14.
Strain: K12.
[5]"Structure and function of YghU, a nu-class glutathione transferase related to YfcG from Escherichia coli."
Stourman N.V., Branch M.C., Schaab M.R., Harp J.M., Ladner J.E., Armstrong R.N.
Biochemistry 50:1274-1281(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FAMILY NAME.
Strain: K12.
[6]"Analysis of the structure and function of YfcG from Escherichia coli reveals an efficient and unique disulfide bond reductase."
Wadington M.C., Ladner J.E., Stourman N.V., Harp J.M., Armstrong R.N.
Biochemistry 48:6559-6561(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE DISULFIDE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, SUBUNIT, MUTAGENESIS OF CYS-166.
Strain: K12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC75362.1.
AP009048 Genomic DNA. Translation: BAA16139.1.
PIRD65002.
RefSeqNP_416805.1. NC_000913.3.
YP_490544.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GX0X-ray2.30A1-215[»]
ProteinModelPortalP77526.
SMRP77526. Positions 1-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP77526. 2 interactions.
STRING511145.b2302.

Proteomic databases

PaxDbP77526.
PRIDEP77526.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75362; AAC75362; b2302.
BAA16139; BAA16139; BAA16139.
GeneID12931523.
946763.
KEGGecj:Y75_p2268.
eco:b2302.
PATRIC32119975. VBIEscCol129921_2397.

Organism-specific databases

EchoBASEEB3863.
EcoGeneEG14110. yfcG.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125752.
KOK00799.
OMATYPWVVS.
OrthoDBEOG6677PW.
PhylomeDBP77526.

Enzyme and pathway databases

BioCycEcoCyc:G7194-MONOMER.
ECOL316407:JW2299-MONOMER.
MetaCyc:G7194-MONOMER.
RETL1328306-WGS:GSTH-836-MONOMER.

Gene expression databases

GenevestigatorP77526.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP77526.
PROP77526.

Entry information

Entry nameYFCG_ECOLI
AccessionPrimary (citable) accession number: P77526
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene