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Protein

Disulfide-bond oxidoreductase YfcG

Gene

yfcG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Kineticsi

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.

  1. KM=1.6 mM for glutathione (when assaying the disulfide-bond reductase activity with 2-hydroxyethyl disulfide)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei11 – 111Glutathione 1
    Binding sitei38 – 381Glutathione 1
    Binding sitei52 – 521Glutathione 1; via amide nitrogen and carbonyl oxygen
    Binding sitei132 – 1321Glutathione 2

    GO - Molecular functioni

    • disulfide oxidoreductase activity Source: EcoCyc
    • peroxidase activity Source: UniProtKB-KW

    GO - Biological processi

    • response to oxidative stress Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:yfcG
    Ordered Locus Names:b2302, JW2299
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14110. yfcG.

    Pathology & Biotechi

    Disruption phenotypei

    Deletion of yfcG decreases the resistance of the bacteria to hydrogen peroxide.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91T → A: No effect on GSH transferase activity. 1 Publication
    Mutagenesisi11 – 111N → A: Loss of GSH transferase activity. 1 Publication
    Mutagenesisi14 – 141K → A: 10-fold reduction in GSH transferase activity. 1 Publication
    Mutagenesisi166 – 1661C → A: No effect on disulfide-bond reductase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 215215Disulfide-bond oxidoreductase YfcGPRO_0000186016Add
    BLAST

    Proteomic databases

    PaxDbiP77526.
    PRIDEiP77526.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP77526. 2 interactions.
    STRINGi511145.b2302.

    Structurei

    Secondary structure

    1
    215
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Helixi10 – 2213Combined sources
    Beta strandi26 – 305Combined sources
    Turni33 – 364Combined sources
    Helixi37 – 393Combined sources
    Helixi41 – 444Combined sources
    Beta strandi54 – 596Combined sources
    Beta strandi67 – 715Combined sources
    Helixi72 – 8312Combined sources
    Helixi91 – 10616Combined sources
    Helixi108 – 12013Combined sources
    Helixi127 – 15024Combined sources
    Beta strandi156 – 1583Combined sources
    Helixi161 – 17010Combined sources
    Helixi171 – 1766Combined sources
    Helixi180 – 1823Combined sources
    Helixi184 – 19411Combined sources
    Helixi197 – 2037Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GX0X-ray2.30A1-215[»]
    ProteinModelPortaliP77526.
    SMRiP77526. Positions 1-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP77526.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8787GST N-terminalAdd
    BLAST
    Domaini90 – 215126GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni71 – 722Glutathione 1 binding

    Sequence similaritiesi

    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000125752.
    InParanoidiP77526.
    KOiK00799.
    OMAiPWIVPWE.
    OrthoDBiEOG6677PW.
    PhylomeDBiP77526.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P77526-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIDLYFAPTP NGHKITLFLE EAELDYRLIK VDLGKGGQFR PEFLRISPNN
    60 70 80 90 100
    KIPAIVDHSP ADGGEPLSLF ESGAILLYLA EKTGLFLSHE TRERAATLQW
    110 120 130 140 150
    LFWQVGGLGP MLGQNHHFNH AAPQTIPYAI ERYQVETQRL YHVLNKRLEN
    160 170 180 190 200
    SPWLGGENYS IADIACWPWV NAWTRQRIDL AMYPAVKNWH ERIRSRPATG
    210
    QALLKAQLGD ERSDS
    Length:215
    Mass (Da):24,516
    Last modified:February 1, 1997 - v1
    Checksum:i058CEBAC879A3050
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75362.1.
    AP009048 Genomic DNA. Translation: BAA16139.1.
    PIRiD65002.
    RefSeqiNP_416805.1. NC_000913.3.
    WP_000566471.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75362; AAC75362; b2302.
    BAA16139; BAA16139; BAA16139.
    GeneIDi946763.
    KEGGieco:b2302.
    PATRICi32119975. VBIEscCol129921_2397.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75362.1.
    AP009048 Genomic DNA. Translation: BAA16139.1.
    PIRiD65002.
    RefSeqiNP_416805.1. NC_000913.3.
    WP_000566471.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GX0X-ray2.30A1-215[»]
    ProteinModelPortaliP77526.
    SMRiP77526. Positions 1-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP77526. 2 interactions.
    STRINGi511145.b2302.

    Proteomic databases

    PaxDbiP77526.
    PRIDEiP77526.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75362; AAC75362; b2302.
    BAA16139; BAA16139; BAA16139.
    GeneIDi946763.
    KEGGieco:b2302.
    PATRICi32119975. VBIEscCol129921_2397.

    Organism-specific databases

    EchoBASEiEB3863.
    EcoGeneiEG14110. yfcG.

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000125752.
    InParanoidiP77526.
    KOiK00799.
    OMAiPWIVPWE.
    OrthoDBiEOG6677PW.
    PhylomeDBiP77526.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP77526.
    PROiP77526.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
      , 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. 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.

    Entry informationi

    Entry nameiYFCG_ECOLI
    AccessioniPrimary (citable) accession number: P77526
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: July 22, 2015
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.1 Publication
    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- (PubMed:19537707).1 Publication

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.