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P77526

- YFCG_ECOLI

UniProt

P77526 - YFCG_ECOLI

Protein

Disulfide-bond oxidoreductase YfcG

Gene

yfcG

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    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

    1. disulfide oxidoreductase activity Source: EcoCyc
    2. peroxidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. response to oxidative stress Source: EcoCyc

    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: Chromosome, UP000000625: 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.

    Expressioni

    Gene expression databases

    GenevestigatoriP77526.

    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 – 65
    Helixi10 – 2213
    Beta strandi26 – 305
    Turni33 – 364
    Helixi37 – 393
    Helixi41 – 444
    Beta strandi54 – 596
    Beta strandi67 – 715
    Helixi72 – 8312
    Helixi91 – 10616
    Helixi108 – 12013
    Helixi127 – 15024
    Beta strandi156 – 1583
    Helixi161 – 17010
    Helixi171 – 1766
    Helixi180 – 1823
    Helixi184 – 19411
    Helixi197 – 2037

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK00799.
    OMAiTYPWVVS.
    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

    MIDLYFAPTP NGHKITLFLE EAELDYRLIK VDLGKGGQFR PEFLRISPNN    50
    KIPAIVDHSP ADGGEPLSLF ESGAILLYLA EKTGLFLSHE TRERAATLQW 100
    LFWQVGGLGP MLGQNHHFNH AAPQTIPYAI ERYQVETQRL YHVLNKRLEN 150
    SPWLGGENYS IADIACWPWV NAWTRQRIDL AMYPAVKNWH ERIRSRPATG 200
    QALLKAQLGD ERSDS 215
    Length:215
    Mass (Da):24,516
    Last modified:February 1, 1997 - v1
    Checksum:i058CEBAC879A3050
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75362.1.
    AP009048 Genomic DNA. Translation: BAA16139.1.
    PIRiD65002.
    RefSeqiNP_416805.1. NC_000913.3.
    YP_490544.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75362; AAC75362; b2302.
    BAA16139; BAA16139; BAA16139.
    GeneIDi12931523.
    946763.
    KEGGiecj:Y75_p2268.
    eco:b2302.
    PATRICi32119975. VBIEscCol129921_2397.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75362.1 .
    AP009048 Genomic DNA. Translation: BAA16139.1 .
    PIRi D65002.
    RefSeqi NP_416805.1. NC_000913.3.
    YP_490544.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GX0 X-ray 2.30 A 1-215 [» ]
    ProteinModelPortali P77526.
    SMRi P77526. Positions 1-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P77526. 2 interactions.
    STRINGi 511145.b2302.

    Proteomic databases

    PaxDbi P77526.
    PRIDEi P77526.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75362 ; AAC75362 ; b2302 .
    BAA16139 ; BAA16139 ; BAA16139 .
    GeneIDi 12931523.
    946763.
    KEGGi ecj:Y75_p2268.
    eco:b2302.
    PATRICi 32119975. VBIEscCol129921_2397.

    Organism-specific databases

    EchoBASEi EB3863.
    EcoGenei EG14110. yfcG.

    Phylogenomic databases

    eggNOGi COG0625.
    HOGENOMi HOG000125752.
    KOi K00799.
    OMAi TYPWVVS.
    OrthoDBi EOG6677PW.
    PhylomeDBi P77526.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei P77526.
    PROi P77526.

    Gene expression databases

    Genevestigatori P77526.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 104 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